|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
5-437 |
0e+00 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 819.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 5 TFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSGPPRVLVVTP 84
Cdd:PRK11192 2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGPPRILILTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 85 TRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLD 164
Cdd:PRK11192 82 TRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 165 MGFANDIETIAGETRWRKQTMLFSATLEGEAIRDFAERLLEDPIEIDADPSRRERKKIQQFHYRADTLEHKTALLCHLLK 244
Cdd:PRK11192 162 MGFAQDIETIAAETRWRKQTLLFSATLEGDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYYRADDLEHKTALLCHLLK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 245 QDEVTKAIVFVRKRERLRELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIENVSHVFNFD 324
Cdd:PRK11192 242 QPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 325 LPRTADVYLHRIGRTGRAGRKGTAISLVEAHDFPLFGKITRYIEEPIKIRVVDSLRPTTKAPSEAmlNKPKPSKKVLAKR 404
Cdd:PRK11192 322 MPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKARVIDELRPKTKAPSEK--KTGKPSKKVLAKR 399
|
410 420 430
....*....|....*....|....*....|...
gi 1468173135 405 KEKKKEEQAKKKEKVRHRDKKNIGKRRTPVSSS 437
Cdd:PRK11192 400 AEKKEKEKEKPKVKKRHRDTKNIGKRRKPSGTS 432
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
5-431 |
4.46e-167 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 476.18 E-value: 4.46e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 5 TFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLdfpRKKSGPPRVLVVTP 84
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLD---PSRPRAPQALILAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 85 TRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLD 164
Cdd:COG0513 80 TRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 165 MGFANDIETIAGETRWRKQTMLFSATLEGEaIRDFAERLLEDPIEIDADPSRRERKKIQQFHYRADTlEHKTALLCHLLK 244
Cdd:COG0513 160 MGFIEDIERILKLLPKERQTLLFSATMPPE-IRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDK-RDKLELLRRLLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 245 QDEVTKAIVFVRKRERLRELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIENVSHVFNFD 324
Cdd:COG0513 238 DEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 325 LPRTADVYLHRIGRTGRAGRKGTAISLVEAHDFPLFGKITRYIEEPIKIRVVDSLRPTTKAPSEAMLNKPKPSKKvlakr 404
Cdd:COG0513 318 LPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEPVEEKRLERLKPKIKEKLK----- 392
|
410 420
....*....|....*....|....*..
gi 1468173135 405 KEKKKEEQAKKKEKVRHRDKKNIGKRR 431
Cdd:COG0513 393 GKKAGRGGRPGPKGERKARRGKRRRRK 419
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-389 |
2.55e-90 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 281.69 E-value: 2.55e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 1 MTASTFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHL-LDFPRKKSgpprv 79
Cdd:PRK11776 1 MSMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLdVKRFRVQA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 80 LVVTPTRELAMQVADQAKEL--CAHNhLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILD 157
Cdd:PRK11776 76 LVLCPTRELADQVAKEIRRLarFIPN-IKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 158 EADRMLDMGFANDIETIAGETRWRKQTMLFSATLeGEAIRDFAERLLEDPIEIDADpSRRERKKIQQFHYRADTlEHKTA 237
Cdd:PRK11776 155 EADRMLDMGFQDAIDAIIRQAPARRQTLLFSATY-PEGIAAISQRFQRDPVEVKVE-STHDLPAIEQRFYEVSP-DERLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 238 LLCHLLKQDEVTKAIVFVRKRERLRELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIENV 317
Cdd:PRK11776 232 ALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKAL 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1468173135 318 SHVFNFDLPRTADVYLHRIGRTGRAGRKGTAISLVEAHDFPLFGKITRYIEEPIKIRVVDSLRPTTKAPSEA 389
Cdd:PRK11776 312 EAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLP 383
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
1-398 |
4.14e-88 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 274.54 E-value: 4.14e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 1 MTASTFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFP---RKKSGPP 77
Cdd:PRK04837 5 LTEQKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPapeDRKVNQP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 78 RVLVVTPTRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILD 157
Cdd:PRK04837 85 RALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 158 EADRMLDMGFANDIetiagetRW--RKQ-------TMLFSATLEGEaIRDFAERLLEDPIEIDADPSRRERKKIQQ--FH 226
Cdd:PRK04837 165 EADRMFDLGFIKDI-------RWlfRRMppanqrlNMLFSATLSYR-VRELAFEHMNNPEYVEVEPEQKTGHRIKEelFY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 227 yraDTLEHKTALLCHLLKQDEVTKAIVFVRKRERLRELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQVKVLVATD 306
Cdd:PRK04837 237 ---PSNEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 307 VASRGLDIENVSHVFNFDLPRTADVYLHRIGRTGRAGRKGTAISLV-EAHDFPLfGKITRYIEEPIkirvvdslrPTTKA 385
Cdd:PRK04837 314 VAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLAcEEYALNL-PAIETYIGHSI---------PVSKY 383
|
410
....*....|....
gi 1468173135 386 PSEAMLNK-PKPSK 398
Cdd:PRK04837 384 DSDALLTDlPKPLR 397
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
15-211 |
1.11e-82 |
|
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: 252.75 E-value: 1.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 15 LINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSGPPRVLVVTPTRELAMQVAD 94
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 95 QAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLDMGFANDIETI 174
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1468173135 175 AGETRWRKQTMLFSATLEgEAIRDFAERLLEDPIEID 211
Cdd:cd00268 161 LSALPKDRQTLLFSATLP-EEVKELAKKFLKNPVRIE 196
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
2-393 |
1.23e-82 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 266.71 E-value: 1.23e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 2 TASTFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIqHLLDfPRKKSgpPRVLV 81
Cdd:PRK11634 4 FETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLL-HNLD-PELKA--PQILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 82 VTPTRELAMQVADQAKELCAHNH-LDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEAD 160
Cdd:PRK11634 80 LAPTRELAVQVAEAMTDFSKHMRgVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 161 RMLDMGFANDIETIAGETRWRKQTMLFSATLEgEAIRDFAERLLEDPIEIDADPSRRERKKIQQFHYRADTLEhKTALLC 240
Cdd:PRK11634 160 EMLRMGFIEDVETIMAQIPEGHQTALFSATMP-EAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMR-KNEALV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 241 HLLKQDEVTKAIVFVRKRERLRELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIENVSHV 320
Cdd:PRK11634 238 RFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLV 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1468173135 321 FNFDLPRTADVYLHRIGRTGRAGRKGTAISLVEAHDFPLFgkitRYIEEPIKIRVVDSLRPTTKAPSEAMLNK 393
Cdd:PRK11634 318 VNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLL----RNIERTMKLTIPEVELPNAELLGKRRLEK 386
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
5-392 |
5.16e-79 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 252.42 E-value: 5.16e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 5 TFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSG--PPRVLVV 82
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKGrrPVRALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 83 TPTRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRM 162
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 163 LDMGFANDIETIAGETRWRKQTMLFSATLEGEaIRDFAERLLEDPIEIDADPSRRERKKIQQFHYRADTlEHKTALLCHL 242
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDD-IKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDK-KRKRELLSQM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 243 LKQDEVTKAIVFVRKRERLRELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIENVSHVFN 322
Cdd:PRK10590 240 IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 323 FDLPRTADVYLHRIGRTGRAGRKGTAISLVEAHDFPLFGKITRYIEEPIKIRVVDSLRPTTKAPSEAMLN 392
Cdd:PRK10590 320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIPRIAIPGYEPDPSIKAEPIQN 389
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
3-356 |
6.30e-79 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 252.53 E-value: 6.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 3 ASTFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKS---GPPRV 79
Cdd:PRK01297 86 KTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPKErymGEPRA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 80 LVVTPTRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQ-DIVVATTGRLLQYIKEENFDCRAVEILILDE 158
Cdd:PRK01297 166 LIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARFcDILVATPGRLLDFNQRGEVHLDMVEVMVLDE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 159 ADRMLDMGFANDIETIAGET--RWRKQTMLFSATLEgEAIRDFAERLLEDPIEIDADPSRRERKKIQQfHYRADTLEHKT 236
Cdd:PRK01297 246 ADRMLDMGFIPQVRQIIRQTprKEERQTLLFSATFT-DDVMNLAKQWTTDPAIVEIEPENVASDTVEQ-HVYAVAGSDKY 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 237 ALLCHLLKQDEVTKAIVFVRKRERLRELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIEN 316
Cdd:PRK01297 324 KLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDG 403
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1468173135 317 VSHVFNFDLPRTADVYLHRIGRTGRAGRKGTAISLVEAHD 356
Cdd:PRK01297 404 ISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
1-386 |
7.38e-76 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 247.17 E-value: 7.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 1 MTASTFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFP---RKKSGPP 77
Cdd:PRK04537 6 LTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPalaDRKPEDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 78 RVLVVTPTRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKE-ENFDCRAVEILIL 156
Cdd:PRK04537 86 RALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHACEICVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 157 DEADRMLDMGFANDIETIAGET--RWRKQTMLFSATLEGEAIrDFAERLLEDP----IEIDADPSRRERKKIqqfHYRAD 230
Cdd:PRK04537 166 DEADRMFDLGFIKDIRFLLRRMpeRGTRQTLLFSATLSHRVL-ELAYEHMNEPeklvVETETITAARVRQRI---YFPAD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 231 tlEHKTALLCHLLKQDEVTKAIVFVRKRERLRELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQVKVLVATDVASR 310
Cdd:PRK04537 242 --EEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 311 GLDIENVSHVFNFDLPRTADVYLHRIGRTGRAGRKGTAISLV---EAHDFPlfgKITRYIEEPIKIRVVDS--LRPTTKA 385
Cdd:PRK04537 320 GLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFAcerYAMSLP---DIEAYIEQKIPVEPVTAelLTPLPRP 396
|
.
gi 1468173135 386 P 386
Cdd:PRK04537 397 P 397
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
5-371 |
3.43e-64 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 215.79 E-value: 3.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 5 TFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSGP-PRVLVVT 83
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQPLLRYGDgPIVLVLA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 84 PTRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRML 163
Cdd:PTZ00110 211 PTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRML 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 164 DMGFANDIETIAGETRWRKQTMLFSATLEGEAIRDFAERLLEDPIEI-----DADPSRRerkkIQQFHYRADTLEhKTAL 238
Cdd:PTZ00110 291 DMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEEPVHVnvgslDLTACHN----IKQEVFVVEEHE-KRGK 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 239 LCHLLKQ--DEVTKAIVFVRKRERLRELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIEN 316
Cdd:PTZ00110 366 LKMLLQRimRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKD 445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1468173135 317 VSHVFNFDLPRTADVYLHRIGRTGRAGRKGTAISLVEAHDFPL---FGKITRYIEEPI 371
Cdd:PTZ00110 446 VKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLardLVKVLREAKQPV 503
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
5-369 |
7.99e-61 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 203.13 E-value: 7.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 5 TFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQhLLDFPRKKSgppRVLVVTP 84
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQ-LIDYDLNAC---QALILAP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 85 TRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLD 164
Cdd:PTZ00424 105 TRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 165 MGFANDIETIAGETRWRKQTMLFSATLEGEaIRDFAERLLEDPIEIDADPSRRERKKIQQFHYRADTLEHKTALLCHLLK 244
Cdd:PTZ00424 185 RGFKGQIYDVFKKLPPDVQVALFSATMPNE-ILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 245 QDEVTKAIVFVRKRERLRELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIENVSHVFNFD 324
Cdd:PTZ00424 264 TLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYD 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1468173135 325 LPRTADVYLHRIGRTGRAGRKGTAISLVEAHDFPLFGKITRY----IEE 369
Cdd:PTZ00424 344 LPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHyntqIEE 392
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
222-352 |
2.12e-56 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 182.71 E-value: 2.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 222 IQQFHYRADTLEHKTALLCHLLKQDEVTKAIVFVRKRERLRELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQVKV 301
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1468173135 302 LVATDVASRGLDIENVSHVFNFDLPRTADVYLHRIGRTGRAGRKGTAISLV 352
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
5-360 |
4.32e-55 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 191.15 E-value: 4.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 5 TFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSG---PPRVLV 81
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHPSeqrNPLAMV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 82 VTPTRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADR 161
Cdd:PLN00206 202 LTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDC 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 162 MLDMGFANDIETIAgETRWRKQTMLFSATLEGEaIRDFAERLLEDPIEIDADPSRRERKKIQQFHYRADTLEHKTALLCH 241
Cdd:PLN00206 282 MLERGFRDQVMQIF-QALSQPQVLLFSATVSPE-VEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 242 LL-KQDEVTKAIVFVRKRERLRELVQWLREA-GIEPCYLEGEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIENVSH 319
Cdd:PLN00206 360 LKsKQHFKPPAVVFVSSRLGADLLANAITVVtGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQ 439
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1468173135 320 VFNFDLPRTADVYLHRIGRTGRAGRKGTAISLVEAHDFPLF 360
Cdd:PLN00206 440 VIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLF 480
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
15-211 |
1.51e-53 |
|
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: 177.45 E-value: 1.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 15 LINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSGpPRVLVVTPTRELAMQVAD 94
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAA-TRVLVLVPTRELAMQCFS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 95 QAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEE-NFDCRAVEILILDEADRMLDMGFANDIET 173
Cdd:cd17947 80 VLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSpSFDLDSIEILVLDEADRMLEEGFADELKE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1468173135 174 IAGETRWRKQTMLFSATLeGEAIRDFAERLLEDPIEID 211
Cdd:cd17947 160 ILRLCPRTRQTMLFSATM-TDEVKDLAKLSLNKPVRVF 196
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
5-206 |
3.13e-51 |
|
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: 172.29 E-value: 3.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 5 TFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFP------RKKSGPPR 78
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGppsvgrGRRKAYPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 79 VLVVTPTRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDE 158
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1468173135 159 ADRMLDMGFANDIETIA-------GETRwrkQTMLFSATLEGEaIRDFAERLLED 206
Cdd:cd17967 161 ADRMLDMGFEPQIRKIVehpdmppKGER---QTLMFSATFPRE-IQRLAADFLKN 211
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
39-191 |
4.15e-49 |
|
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: 164.72 E-value: 4.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 39 MDGRDVLGSAPTGTGKTAAFLLPAIQHLldfpRKKSGPPRVLVVTPTRELAMQVADQAKELCAHNHLDIATITGGVAYMN 118
Cdd:pfam00270 12 LEGRDVLVQAPTGSGKTLAFLLPALEAL----DKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLLGGDSRKE 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1468173135 119 HAEVFsENQDIVVATTGRLLQYIKEENFdCRAVEILILDEADRMLDMGFANDIETIAGETRWRKQTMLFSATL 191
Cdd:pfam00270 88 QLEKL-KGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATL 158
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
5-191 |
7.01e-49 |
|
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: 165.57 E-value: 7.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 5 TFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRkksgPPRVLVVTP 84
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQ----RFFALVLAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 85 TRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEEN-FDCRAVEILILDEADRML 163
Cdd:cd17954 77 TRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSLKFLVMDEADRLL 156
|
170 180
....*....|....*....|....*...
gi 1468173135 164 DMGFANDIETIAGETRWRKQTMLFSATL 191
Cdd:cd17954 157 NMDFEPEIDKILKVIPRERTTYLFSATM 184
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
4-210 |
1.53e-48 |
|
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: 164.79 E-value: 1.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 4 STFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDfpRKKSGPPRVLVVT 83
Cdd:cd17959 1 GGFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKA--HSPTVGARALILS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 84 PTRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRML 163
Cdd:cd17959 79 PTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1468173135 164 DMGFANDIETIAGETRWRKQTMLFSATLEgEAIRDFAERLLEDPIEI 210
Cdd:cd17959 159 EMGFAEQLHEILSRLPENRQTLLFSATLP-KLLVEFAKAGLNEPVLI 204
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
11-200 |
3.10e-48 |
|
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: 164.29 E-value: 3.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 11 LDESLINALSDKGYQRPTAIQAAAIPAAM-DGRDVLGSAPTGTGKTAAFLLPAIQHLL-DFPRKKSGPPRVLVVTPTREL 88
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLnTKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 89 AMQVADQAKELCAHNH-LDIATITGGVAYM-NHAEVFSENQDIVVATTGRLLQYIKEENF--DCRAVEILILDEADRMLD 164
Cdd:cd17964 81 ALQIAAEAKKLLQGLRkLRVQSAVGGTSRRaELNRLRRGRPDILVATPGRLIDHLENPGVakAFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1468173135 165 MGFANDIETI------AGETRWrkQTMLFSATLEGEaIRDFA 200
Cdd:cd17964 161 MGFRPDLEQIlrhlpeKNADPR--QTLLFSATVPDE-VQQIA 199
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
15-210 |
1.29e-46 |
|
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: 159.46 E-value: 1.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 15 LINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSGP-PRVLVVTPTRELAMQVA 93
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERGDgPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 94 DQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLDMGFANDIET 173
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1468173135 174 IAGETRWRKQTMLFSATLEGEaIRDFAERLLEDPIEI 210
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKE-VRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
15-210 |
3.07e-46 |
|
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: 158.35 E-value: 3.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 15 LINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSGP-PRVLVVTPTRELAMQVA 93
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKGEgPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 94 DQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLDMGFANDIET 173
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1468173135 174 IAGETRWRKQTMLFSATLEgEAIRDFAERLLEDPIEI 210
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFK-KKIEQLARDILSDPIRV 196
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
42-222 |
6.52e-46 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 157.65 E-value: 6.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 42 RDVLGSAPTGTGKTAAFLLPAIQHLldfprKKSGPPRVLVVTPTRELAMQVADQAKELCAHNHLDIATITGGVAY-MNHA 120
Cdd:smart00487 25 RDVILAAPTGSGKTLAALLPALEAL-----KRGKGGRVLVLVPTRELAEQWAEELKKLGPSLGLKVVGLYGGDSKrEQLR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 121 EVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLDMGFANDIETIAGETRWRKQTMLFSATLEGEaIRDFA 200
Cdd:smart00487 100 KLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKNVQLLLLSATPPEE-IENLL 178
|
170 180
....*....|....*....|..
gi 1468173135 201 ERLLEDPIEIDADPSRRERKKI 222
Cdd:smart00487 179 ELFLNDPVFIDVGFTPLEPIEQ 200
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
18-210 |
4.39e-45 |
|
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: 155.53 E-value: 4.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 18 ALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLdfpRKKSGPPR---VLVVTPTRELAMQVAD 94
Cdd:cd17941 4 GLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLY---RERWTPEDglgALIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 95 QAKELCAHNHLDIATITGGVAYMNHAEVFSEnQDIVVATTGRLLQYIKEE-NFDCRAVEILILDEADRMLDMGFANDIET 173
Cdd:cd17941 81 VLRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1468173135 174 IAGETRWRKQTMLFSATLEgEAIRDFAERLLEDPIEI 210
Cdd:cd17941 160 IVENLPKSRQTLLFSATQT-KSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
6-207 |
1.21e-44 |
|
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: 154.69 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 6 FTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPrkkSGpPRVLVVTPT 85
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDP---YG-IFALVLTPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 86 RELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIK---EENFDCRAVEILILDEADRM 162
Cdd:cd17955 77 RELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1468173135 163 LDMGFANDIETIAGETRWRKQTMLFSATLEgEAIRDFAERLLEDP 207
Cdd:cd17955 157 LTGSFEDDLATILSALPPKRQTLLFSATLT-DALKALKELFGNKP 200
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
4-206 |
8.47e-44 |
|
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: 154.35 E-value: 8.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 4 STFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSG-----PPR 78
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSfsevqEPQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 79 VLVVTPTRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDE 158
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1468173135 159 ADRMLDMGFANDIETIAGETRW----RKQTMLFSATLEGEAIRDFAERLLED 206
Cdd:cd18052 203 ADRMLDMGFGPEIRKLVSEPGMpskeDRQTLMFSATFPEEIQRLAAEFLKED 254
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
15-210 |
9.06e-44 |
|
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: 151.97 E-value: 9.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 15 LINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDfPRKKSGpPRVLVVTPTRELAMQVAD 94
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGK-PRKKKG-LRALILAPTRELASQIYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 95 QAKELCAHNHLDIATITGG-VAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLDMGFANDIET 173
Cdd:cd17957 79 ELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDE 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1468173135 174 I-AGETRWRKQTMLFSATLeGEAIRDFAERLLEDPIEI 210
Cdd:cd17957 159 IlAACTNPNLQRSLFSATI-PSEVEELARSVMKDPIRI 195
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
15-191 |
2.92e-42 |
|
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: 149.31 E-value: 2.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 15 LINALSDKGYQRPTAIQAAAIPAAM-DGRDVLGSAPTGTGKTAAFLLPAIQHLLD-----FPRKKSGPPRVLVVTPTREL 88
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIrDGKDVIGAAETGSGKTLAFGIPILERLLSqkssnGVGGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 89 AMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEEN-FDC--RAVEILILDEADRMLDM 165
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNeHLAnlKSLRFLVLDEADRMLEK 160
|
170 180 190
....*....|....*....|....*....|....
gi 1468173135 166 GFANDIETI--------AGETRWRkQTMLFSATL 191
Cdd:cd17946 161 GHFAELEKIlellnkdrAGKKRKR-QTFVFSATL 193
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
11-191 |
3.36e-41 |
|
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: 145.42 E-value: 3.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 11 LDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSGP--PRVLVVTPTREL 88
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEqgTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 89 AMQVADQAKELCAH--NHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEEN-FDCRAVEILILDEADRMLDM 165
Cdd:cd17961 81 AQQVSKVLEQLTAYcrKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSlLLLSTLKYLVIDEADLVLSY 160
|
170 180
....*....|....*....|....*.
gi 1468173135 166 GFANDIETIAGETRWRKQTMLFSATL 191
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATL 186
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
5-210 |
1.82e-40 |
|
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: 144.06 E-value: 1.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 5 TFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSGP-PRVLVVT 83
Cdd:cd17953 13 KWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPGEgPIGLIMA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 84 PTRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEEN---FDCRAVEILILDEAD 160
Cdd:cd17953 93 PTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNgrvTNLRRVTYVVLDEAD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1468173135 161 RMLDMGFANDIETIAGETRWRKQTMLFSATLEgEAIRDFAERLLEDPIEI 210
Cdd:cd17953 173 RMFDMGFEPQIMKIVNNIRPDRQTVLFSATFP-RKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
18-190 |
3.85e-40 |
|
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: 142.50 E-value: 3.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 18 ALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQ--HLLDF-PRKKSGpprVLVVTPTRELAMQVAD 94
Cdd:cd17942 4 AIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllYKLKFkPRNGTG---VIIISPTRELALQIYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 95 QAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIK-EENFDCRAVEILILDEADRMLDMGFANDIET 173
Cdd:cd17942 81 VAKELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQnTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
|
170
....*....|....*..
gi 1468173135 174 IAGETRWRKQTMLFSAT 190
Cdd:cd17942 161 IIKLLPKRRQTMLFSAT 177
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
15-210 |
7.73e-39 |
|
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: 139.14 E-value: 7.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 15 LINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLL--DFPRKKSGPPRVLVVTPTRELAMQV 92
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDlqPIPREQRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 93 ADQAKELcAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLDMGFANDIE 172
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1468173135 173 TIAGETRWRKQTMLFSATLEgEAIRDFAERLLEDPIEI 210
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWP-DGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
15-211 |
5.25e-38 |
|
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: 137.09 E-value: 5.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 15 LINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLD----FPRKKSGPPRVLVVTPTRELAM 90
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEqekkLPFIKGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 91 QVADQAKELCAH------NHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLD 164
Cdd:cd17951 81 QTHEVIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1468173135 165 MGFANDIETIAGETRWRKQTMLFSATLEgEAIRDFAERLLEDPIEID 211
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMP-KKIQNFAKSALVKPVTVN 206
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
15-210 |
5.68e-38 |
|
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: 137.45 E-value: 5.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 15 LINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFP----RKKSGPPRVLVVTPTRELAM 90
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPpldeETKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 91 QVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLDMGFAND 170
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 171 IETI--------------------AGETRWRKQTMLFSATLEgEAIRDFAERLLEDPIEI 210
Cdd:cd17945 161 VTKIldampvsnkkpdteeaeklaASGKHRYRQTMMFTATMP-PAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
15-191 |
8.92e-38 |
|
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: 136.17 E-value: 8.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 15 LINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDfPRKKSGPPRV--LVVTPTRELAMQV 92
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLK-RKANLKKGQVgaLIISPTRELATQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 93 ADQAKELCAH--NHLDIATITGGVAYMNHAEVFSENQ-DIVVATTGRLLQYI--KEENFDCRAVEILILDEADRMLDMGF 167
Cdd:cd17960 80 YEVLQSFLEHhlPKLKCQLLIGGTNVEEDVKKFKRNGpNILVGTPGRLEELLsrKADKVKVKSLEVLVLDEADRLLDLGF 159
|
170 180
....*....|....*....|....*.
gi 1468173135 168 ANDIETIAGetRWRKQ--TMLFSATL 191
Cdd:cd17960 160 EADLNRILS--KLPKQrrTGLFSATQ 183
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
15-210 |
4.24e-36 |
|
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: 131.52 E-value: 4.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 15 LINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKksgpPRVLVVTPTRELAMQVAD 94
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRN----PSALILTPTRELAVQIED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 95 QAKELC-AHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLDMGFANDIET 173
Cdd:cd17962 77 QAKELMkGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLD 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1468173135 174 IAGETRWRKQTMLFSATLEGEaIRDFAERLLEDPIEI 210
Cdd:cd17962 157 ILENISHDHQTILVSATIPRG-IEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
6-211 |
1.78e-35 |
|
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: 131.28 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 6 FTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSGP-PRVLVVTP 84
Cdd:cd18049 26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDgPICLVLAP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 85 TRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLD 164
Cdd:cd18049 106 TRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1468173135 165 MGFANDIETIAGETRWRKQTMLFSATLEGEaIRDFAERLLEDPIEID 211
Cdd:cd18049 186 MGFEPQIRKIVDQIRPDRQTLMWSATWPKE-VRQLAEDFLKDYIHIN 231
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
8-211 |
3.07e-35 |
|
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: 129.37 E-value: 3.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 8 ELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLlDFPRKKsgpPRVLVVTPTRE 87
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRI-DTTVRE---TQALVLAPTRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 88 LAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLDMGF 167
Cdd:cd17939 77 LAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1468173135 168 ANDIETI----AGETrwrkQTMLFSATLEGEAIRdFAERLLEDPIEID 211
Cdd:cd17939 157 KDQIYDIfqflPPET----QVVLFSATMPHEVLE-VTKKFMRDPVRIL 199
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
15-211 |
1.23e-34 |
|
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: 128.09 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 15 LINALSDK-GYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRK---KSGpPRVLVVTPTRELAM 90
Cdd:cd17949 1 LVSHLKSKmGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvdrSDG-TLALVLVPTRELAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 91 QVADQAKEL--CAHNhLDIATITGGvaymnhaevfsENQD-----------IVVATTGRLLQYIKE-ENFDCRAVEILIL 156
Cdd:cd17949 80 QIYEVLEKLlkPFHW-IVPGYLIGG-----------EKRKsekarlrkgvnILIATPGRLLDHLKNtQSFDVSNLRWLVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1468173135 157 DEADRMLDMGFANDIETIAGETRW-------------RKQTMLFSATLEgEAIRDFAERLLEDPIEID 211
Cdd:cd17949 148 DEADRLLDMGFEKDITKILELLDDkrskaggekskpsRRQTVLVSATLT-DGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
6-211 |
2.97e-34 |
|
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: 127.05 E-value: 2.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 6 FTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLldfprkksgppRVLVVTPT 85
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV-----------VALILEPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 86 RELAMQVADQAKELCAH---NHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRM 162
Cdd:cd17938 70 RELAEQTYNCIENFKKYldnPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1468173135 163 LDMGFANDIETI------AGETRWRKQTMLFSATLEGEAIRDFAERLLEDPIEID 211
Cdd:cd17938 150 LSQGNLETINRIynripkITSDGKRLQVIVCSATLHSFEVKKLADKIMHFPTWVD 204
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
6-211 |
7.31e-34 |
|
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: 127.82 E-value: 7.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 6 FTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSGP-PRVLVVTP 84
Cdd:cd18050 64 FHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGDgPICLVLAP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 85 TRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLD 164
Cdd:cd18050 144 TRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLD 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1468173135 165 MGFANDIETIAGETRWRKQTMLFSATLEGEaIRDFAERLLEDPIEID 211
Cdd:cd18050 224 MGFEPQIRKIVDQIRPDRQTLMWSATWPKE-VRQLAEDFLRDYVQIN 269
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
6-210 |
2.60e-33 |
|
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: 124.33 E-value: 2.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 6 FTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLldfpRKKSGPPRVLVVTPT 85
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI----DPKKDVIQALILVPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 86 RELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLDM 165
Cdd:cd17940 77 RELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1468173135 166 GFANDIETIAGETRWRKQTMLFSATLEgEAIRDFAERLLEDPIEI 210
Cdd:cd17940 157 DFQPIIEKILNFLPKERQILLFSATFP-LTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
15-191 |
1.00e-32 |
|
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: 123.51 E-value: 1.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 15 LINALSDKGYQR---------PTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSgppRVLVVTPT 85
Cdd:cd17956 1 LLKNLQNNGITSafpvqaaviPWLLPSSKSTPPYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRL---RALIVVPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 86 RELAMQVADQAKELCAHNHLDIATITGGVAYMN--------HAEVFSENQDIVVATTGRLLQYIKE-ENFDCRAVEILIL 156
Cdd:cd17956 78 KELVQQVYKVFESLCKGTGLKVVSLSGQKSFKKeqklllvdTSGRYLSRVDILVATPGRLVDHLNStPGFTLKHLRFLVI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1468173135 157 DEADRMLDMGFANDIETIAGET------------------RWRK--QTMLFSATL 191
Cdd:cd17956 158 DEADRLLNQSFQDWLETVMKALgrptapdlgsfgdanlleRSVRplQKLLFSATL 212
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
3-210 |
1.99e-32 |
|
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: 122.07 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 3 ASTFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSgpprVLVV 82
Cdd:cd17950 1 SSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVS----VLVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 83 TPTRELAMQVADQAKELCAH-NHLDIATITGGVAYMNHAEVFSENQ-DIVVATTGRLLQYIKEENFDCRAVEILILDEAD 160
Cdd:cd17950 77 CHTRELAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVLDECD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1468173135 161 RML-DMGFANDIETIAGETRWRKQTMLFSATLEgEAIRDFAERLLEDPIEI 210
Cdd:cd17950 157 KMLeQLDMRRDVQEIFRATPHDKQVMMFSATLS-KEIRPVCKKFMQDPLEI 206
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
235-343 |
2.71e-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: 118.47 E-value: 2.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 235 KTALLCHLLKQDEVTKAIVFVRKRERLrELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDI 314
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKKTL-EAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 1468173135 315 ENVSHVFNFDLPRTADVYLHRIGRTGRAG 343
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
40-190 |
3.45e-31 |
|
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: 118.80 E-value: 3.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 40 DGRDVLGSAPTGTGKTAAFLLPAIQHLL--DFPRKKSGPPRVLVVTPTRELAMQVADQAKELCahNHLDIATITGGVAYM 117
Cdd:cd17944 26 SGKDLIAQARTGTGKTFSFAIPLIEKLQedQQPRKRGRAPKVLVLAPTRELANQVTKDFKDIT--RKLSVACFYGGTPYQ 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1468173135 118 NHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLDMGFANDIETIAGEtRWRK------QTMLFSAT 190
Cdd:cd17944 104 QQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILSV-SYKKdsednpQTLLFSAT 181
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
11-210 |
2.67e-30 |
|
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: 116.14 E-value: 2.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 11 LDESLINALSDKGYQRPTAIQAAAIPAAMDG--RDVLGSAPTGTGKTAAFLLPAIQHLlDfPRKKSgpPRVLVVTPTREL 88
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-D-PTLKS--PQALCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 89 AMQVADQAKELCAHNHLDIA-TITGGVAYMNhaEVFSENqdIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLDM-G 166
Cdd:cd17963 77 ARQIGEVVEKMGKFTGVKVAlAVPGNDVPRG--KKITAQ--IVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqG 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1468173135 167 FANDIETIAGETRWRKQTMLFSATLEgEAIRDFAERLLEDPIEI 210
Cdd:cd17963 153 HGDQSIRIKRMLPRNCQILLFSATFP-DSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
4-208 |
2.39e-29 |
|
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: 115.14 E-value: 2.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 4 STFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLdfprkKSGP------- 76
Cdd:cd18051 21 ETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIY-----EQGPgeslpse 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 77 ----------PRVLVVTPTRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENF 146
Cdd:cd18051 96 sgyygrrkqyPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKI 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 147 DCRAVEILILDEADRMLDMGFANDIETI--------AGEtrwrKQTMLFSATLEGEaIRDFAERLLEDPI 208
Cdd:cd18051 176 GLDYCKYLVLDEADRMLDMGFEPQIRRIveqdtmppTGE----RQTLMFSATFPKE-IQMLARDFLDNYI 240
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
6-210 |
2.73e-28 |
|
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: 110.63 E-value: 2.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 6 FTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQhLLDFPRKKsgpPRVLVVTPT 85
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQ-CLDIQVRE---TQALILSPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 86 RELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLDM 165
Cdd:cd18045 77 RELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1468173135 166 GFANDIETIAGETRWRKQTMLFSATLEGEaIRDFAERLLEDPIEI 210
Cdd:cd18045 157 GFKEQIYDVYRYLPPATQVVLVSATLPQD-ILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
15-210 |
3.38e-28 |
|
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: 110.05 E-value: 3.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 15 LINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLldfpRKKSGPPRVLVVTPTRELAMQVAD 94
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESL----DLERRHPQVLILAPTREIAVQIHD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 95 QAKELCAH-NHLDIATITGGVAYMNHAEVFSENQdIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLDMGFANDIET 173
Cdd:cd17943 77 VFKKIGKKlEGLKCEVFIGGTPVKEDKKKLKGCH-IAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1468173135 174 IAGETRWRKQTMLFSATLEGEAIRDFAeRLLEDPIEI 210
Cdd:cd17943 156 IFSSLPKNKQVIAFSATYPKNLDNLLA-RYMRKPVLV 191
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
6-210 |
5.38e-27 |
|
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: 107.15 E-value: 5.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 6 FTELELDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLlDFPRKKsgpPRVLVVTPT 85
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI-DTSLKA---TQALVLAPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 86 RELAMQVADQAKELCAHNHLDIATITGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLDM 165
Cdd:cd18046 77 RELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1468173135 166 GFANDIETIAGETRWRKQTMLFSATLEGEaIRDFAERLLEDPIEI 210
Cdd:cd18046 157 GFKDQIYDIFQKLPPDTQVVLLSATMPND-VLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
15-168 |
2.37e-25 |
|
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: 103.60 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 15 LINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSGP---PRVLVVTPTRELAMQ 91
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLAEGPfnaPRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1468173135 92 VADQAKELCAHNHLDIATITGG--VAYMNHAEvFSENqDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLDMGFA 168
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGrtKRQIRNPH-FEEV-DILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFN 157
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
262-343 |
2.78e-25 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 98.44 E-value: 2.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 262 RELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIENVSHVFNFDLPRTADVYLHRIGRTGR 341
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 1468173135 342 AG 343
Cdd:smart00490 81 AG 82
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
40-375 |
3.14e-22 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 99.33 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 40 DGRDVLGSAPTGTGKTAAFLLpAIQHLLDfprkksgPPRVLVVTPTRELAMQVADQAKElcahnHLDIATITGGvaymnh 119
Cdd:COG1061 99 GGGRGLVVAPTGTGKTVLALA-LAAELLR-------GKRVLVLVPRRELLEQWAEELRR-----FLGDPLAGGG------ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 120 aeVFSENQDIVVATTGRLLQYIKEENFDcRAVEILILDEADRMLDMGFANDIETIAGETR-------WRK-QTMLFSATL 191
Cdd:COG1061 160 --KKDSDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHHAGAPSYRRILEAFPAAYRlgltatpFRSdGREILLFLF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 192 EGEAIRDFAERLLED---------PIEIDADPSRRERKKIQQFHYR--ADTLEHKTALLCHLLKQD-EVTKAIVFVRKRE 259
Cdd:COG1061 237 DGIVYEYSLKEAIEDgylappeyyGIRVDLTDERAEYDALSERLREalAADAERKDKILRELLREHpDDRKTLVFCSSVD 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 260 RLRELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIENVSHVFNFDLPRTADVYLHRIGRT 339
Cdd:COG1061 317 HAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRG 396
|
330 340 350
....*....|....*....|....*....|....*...
gi 1468173135 340 GRAGRKGTAISLVE--AHDFPLFGKITRYIEEPIKIRV 375
Cdd:COG1061 397 LRPAPGKEDALVYDfvGNDVPVLEELAKDLRDLAGYRV 434
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
41-190 |
5.86e-19 |
|
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: 83.22 E-value: 5.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 41 GRDVLGSAPTGTGKTAAFLLPAIQHLLDFprkksgPPRVLVVTPTRELAMQVADQAKELCAHNhLDIATITGGVAYMNHA 120
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLKK------GKKVLVLVPTKALALQTAERLRELFGPG-IRVAVLVGGSSAEERE 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1468173135 121 EVFSENQDIVVATTGRLLQYIKEENFDC-RAVEILILDEADRMLDMGFANDIETIAGETRWRK--QTMLFSAT 190
Cdd:cd00046 74 KNKLGDADIIIATPDMLLNLLLREDRLFlKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKnaQVILLSAT 146
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
11-359 |
1.27e-18 |
|
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: 88.74 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 11 LDESLINALSDKGYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRkksgpPRVLVVTPTRELAm 90
Cdd:COG1205 41 LPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPG-----ATALYLYPTKALA- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 91 qvADQAK---ELCAHNHLDI--ATITGGVAYMNHAEVFsENQDIVVAT-----TGRLLQYIKEENFdCRAVEILILDEA- 159
Cdd:COG1205 115 --RDQLRrlrELAEALGLGVrvATYDGDTPPEERRWIR-EHPDIVLTNpdmlhYGLLPHHTRWARF-FRNLRYVVIDEAh 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 160 --------------DRMLDmgfandietIAGETRWRKQTMLFSATLeGEAiRDFAERLLEDPIE-IDADPSRRERKKI-- 222
Cdd:COG1205 191 tyrgvfgshvanvlRRLRR---------ICRHYGSDPQFILASATI-GNP-AEHAERLTGRPVTvVDEDGSPRGERTFvl 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 223 -----QQFHYRADTLEHKTALLCHLLKQDevTKAIVFVRKReRLRELV-QWLREAGIEPC-----------YLEGEmpqa 285
Cdd:COG1205 260 wnpplVDDGIRRSALAEAARLLADLVREG--LRTLVFTRSR-RGAELLaRYARRALREPDladrvaayragYLPEE---- 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1468173135 286 kRNEAVRRLVDGQVKVLVATDVASRGLDIENVSHVFNFDLPRTADVYLHRIGRTGRAGRKGTAIsLVeAHDFPL 359
Cdd:COG1205 333 -RREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LV-AGDDPL 403
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
2-207 |
6.71e-16 |
|
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: 76.60 E-value: 6.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 2 TASTFTELELDESLINALSDKGYQRPTAIQAAAIPAAMDG--RDVLGSAPTGTGKTAAFLLPAIQHLldfpRKKSGPPRV 79
Cdd:cd18048 16 SVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV----DALKLYPQC 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 80 LVVTPTRELAMQ---VADQAKELCAHNHLDIATITGGVAYMNHAEvfsenQDIVVATTGRLLQY-IKEENFDCRAVEILI 155
Cdd:cd18048 92 LCLSPTFELALQtgkVVEEMGKFCVGIQVIYAIRGNRPGKGTDIE-----AQIVIGTPGTVLDWcFKLRLIDVTNISVFV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1468173135 156 LDEADRMLDM-GFANDIETIAGETRWRKQTMLFSATLEgEAIRDFAERLLEDP 207
Cdd:cd18048 167 LDEADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFE-DSVWAFAERIVPDP 218
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
25-191 |
2.04e-15 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 75.49 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 25 QRPTAIQAAAIPAAMDGRDV-LGSAPTGTGKTAAFLLPAIQHLLDF-------------PRKKSGPPRVLVVTPTRELAM 90
Cdd:cd17965 44 KTLMRKVTKQTSNEEPKLEVfLLAAETGSGKTLAYLAPLLDYLKRQeqepfeeaeeeyeSAKDTGRPRSVILVPTHELVE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 91 QVADQAKELCAHNHLDIATI--TGGVAYMNHAEVFSENQDIVVATTGRLLQYIKEENFDCRAVEILILDEADRMLDMGFA 168
Cdd:cd17965 124 QVYSVLKKLSHTVKLGIKTFssGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFL 203
|
170 180
....*....|....*....|...
gi 1468173135 169 NDIETIAGETRWRKQTMLFSATL 191
Cdd:cd17965 204 QDTTSIIKRAPKLKHLILCSATI 226
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
5-207 |
1.30e-14 |
|
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: 72.45 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 5 TFTELELDESLINALSDKGYQRPTAIQAAAIPAAM--DGRDVLGSAPTGTGKTAAFLLPAIQHlLDFPRKKSgppRVLVV 82
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLaePPQNLIAQSQSGTGKTAAFVLAMLSQ-VEPANKYP---QCLCL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 83 TPTRELAMQVADQAKELCA-HNHLDIATITGGVAYMNHAEVfseNQDIVVATTGRLLQY-IKEENFDCRAVEILILDEAD 160
Cdd:cd18047 78 SPTYELALQTGKVIEQMGKfYPELKLAYAVRGNKLERGQKI---SEQIVIGTPGTVLDWcSKLKFIDPKKIKVFVLDEAD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1468173135 161 RMLDMGFANDiETIAGETRWRK--QTMLFSATLEgEAIRDFAERLLEDP 207
Cdd:cd18047 155 VMIATQGHQD-QSIRIQRMLPRncQMLLFSATFE-DSVWKFAQKVVPDP 201
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
39-356 |
2.18e-12 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 68.63 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 39 MDGRDVLGSAPTGTGKTAAFLLPAIqhLLDfprkksGPprVLVVTPTreLA-MQvaDQAKELCAHnhldiatitgGV--A 115
Cdd:COG0514 30 LAGRDALVVMPTGGGKSLCYQLPAL--LLP------GL--TLVVSPL--IAlMK--DQVDALRAA----------GIraA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 116 YMNHAEVFSENQDI---VVATTGRLLqYI------KEENFD-CRAVEI--LILDEA--------D-----RMLDMgFAND 170
Cdd:COG0514 86 FLNSSLSAEERREVlraLRAGELKLL-YVaperllNPRFLElLRRLKIslFAIDEAhcisqwghDfrpdyRRLGE-LRER 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 171 IETIagetrwrkQTMLFSATLEGEAIRDFAERL-LEDPIEIDADPsrrERKKIQqFHYRADTLEHKTALLCHLLKQDEVT 249
Cdd:COG0514 164 LPNV--------PVLALTATATPRVRADIAEQLgLEDPRVFVGSF---DRPNLR-LEVVPKPPDDKLAQLLDFLKEHPGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 250 KAIVFVRKRERLRELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQVKVLVATdVA-SRGLDIENVSHVFNFDLPRT 328
Cdd:COG0514 232 SGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKS 310
|
330 340
....*....|....*....|....*...
gi 1468173135 329 ADVYLHRIGRTGRAGRKGTAISLVEAHD 356
Cdd:COG0514 311 IEAYYQEIGRAGRDGLPAEALLLYGPED 338
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
194-352 |
1.36e-11 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 66.68 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 194 EAIRDFAERLLE---DPIEIDADPSRRERKKIQQFHYRADTL--EH-KTALLCHLLKQ----DEVTKAIVFVRKRERLRE 263
Cdd:COG1111 289 EALLRYLERLEEearSSGGSKASKRLVSDPRFRKAMRLAEEAdiEHpKLSKLREILKEqlgtNPDSRIIVFTQYRDTAEM 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 264 LVQWLREAGIEPCYLEGE--------MPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIENVSHVFNFDLPRTADVYLHR 335
Cdd:COG1111 369 IVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQR 448
|
170
....*....|....*..
gi 1468173135 336 IGRTGRaGRKGTAISLV 352
Cdd:COG1111 449 KGRTGR-KREGRVVVLI 464
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
250-345 |
5.54e-11 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 64.48 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 250 KAIVFVRKRERLRELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQ--VKVLVATDVASRGLDIENVSHVFNFDLPR 327
Cdd:COG0553 551 KVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLWW 630
|
90
....*....|....*...
gi 1468173135 328 TADVYLHRIGRTGRAGRK 345
Cdd:COG0553 631 NPAVEEQAIDRAHRIGQT 648
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
230-342 |
1.14e-10 |
|
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: 59.53 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 230 DTLEHKTALLCHLLK----QDEVTKAIVFVRKRERLRELVQWLREAGIE-----PCYLEG----------EMPQAKRNEA 290
Cdd:cd18802 3 IVVIPKLQKLIEILReyfpKTPDFRGIIFVERRATAVVLSRLLKEHPSTlafirCGFLIGrgnssqrkrsLMTQRKQKET 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1468173135 291 VRRLVDGQVKVLVATDVASRGLDIENVSHVFNFDLPRTADVYLHRIGRtGRA 342
Cdd:cd18802 83 LDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
235-337 |
2.08e-10 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 58.26 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 235 KTALLCHLLKQ--DEVTKAIVFVRKRERLRELVQWLREAGIEPCYLEGEMPQAKRNEAVRRL-VDGQVKV-LVATDVASR 310
Cdd:cd18793 12 KLEALLELLEElrEPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFnEDPDIRVfLLSTKAGGV 91
|
90 100 110
....*....|....*....|....*....|....*
gi 1468173135 311 GLDIENVSHVFNFDLP--------RTADVylHRIG 337
Cdd:cd18793 92 GLNLTAANRVILYDPWwnpaveeqAIDRA--HRIG 124
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
40-211 |
2.42e-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: 59.20 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 40 DGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKksgpprVLVVTPTRELAMQVADQAKELCAHNHLDIATITGGVAYMNH 119
Cdd:cd17921 16 SGDSVLVSAPTSSGKTLIAELAILRALATSGGK------AVYIAPTRALVNQKEADLRERFGPLGKNVGLLTGDPSVNKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 120 AEvfsENQDIVVATTGRLLQYI-KEENFDCRAVEILILDEADRMLDMGFANDIETIAGETRWRKQTMLF---SATLEGea 195
Cdd:cd17921 90 LL---AEADILVATPEKLDLLLrNGGERLIQDVRLVVVDEAHLIGDGERGVVLELLLSRLLRINKNARFvglSATLPN-- 164
|
170
....*....|....*..
gi 1468173135 196 IRDFAERL-LEDPIEID 211
Cdd:cd17921 165 AEDLAEWLgVEDLIRFD 181
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
41-107 |
6.34e-10 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 57.98 E-value: 6.34e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1468173135 41 GRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKksgPPRVLVVTPTRELAMQVADQAKELCAHNHLDI 107
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEK---GVQVLYISPLKALINDQERRLEEPLDEIDLEI 64
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
220-351 |
7.16e-10 |
|
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: 56.98 E-value: 7.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 220 KKIQQFHYRadtLEHKTALLC-HLLKQDEV--TKAIVFVRKRERLRELVQWLRE--AGIEPCYLEGE--------MPQAK 286
Cdd:cd18801 2 RKVEKIHPK---LEKLEEIVKeHFKKKQEGsdTRVIIFSEFRDSAEEIVNFLSKirPGIRATRFIGQasgksskgMSQKE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1468173135 287 RNEAVRRLVDGQVKVLVATDVASRGLDIENVSHVFNFDLPRTADVYLHRIGRTGRaGRKGTAISL 351
Cdd:cd18801 79 QKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVVVL 142
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
48-345 |
1.05e-09 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 59.75 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 48 APTGTGKTAAFLLPAIQHLldfprKKSGPPRVLVVTPTRELAMQVADQAKELCAHNHLDIATITGGVAYMN-HAEVFSEN 126
Cdd:cd09639 6 APTGYGKTEAALLWALHSL-----KSQKADRVIIALPTRATINAMYRRAKEAFGETGLYHSSILSSRIKEMgDSEEFEHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 127 QDIVVATTGRLLQYI---------------KEENFDCRAVEI----LILDEADRMLDMGFANDIETIAGETRWRKQTMLF 187
Cdd:cd09639 81 FPLYIHSNDTLFLDPitvctidqvlksvfgEFGHYEFTLASIanslLIFDEVHFYDEYTLALILAVLEVLKDNDVPILLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 188 SATLEgeairDFAERLLEDpIEIDADPSRRERKKIQQFHYR---ADTLEHKTALLCHLLKQDEVTKAIVFVRKRERLREL 264
Cdd:cd09639 161 SATLP-----KFLKEYAEK-IGYVEENEPLDLKPNERAPFIkieSDKVGEISSLERLLEFIKKGGSVAIIVNTVDRAQEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 265 VQWLREAGIEP--CYLEGEMPQA----KRNEAVRRLVDGQVKVLVATDVASRGLDIenvshvfNFDL----PRTADVYLH 334
Cdd:cd09639 235 YQQLKEKGPEEeiMLIHSRFTEKdrakKEAELLLEFKKSEKFVIVATQVIEASLDI-------SVDVmiteLAPIDSLIQ 307
|
330
....*....|.
gi 1468173135 335 RIGRTGRAGRK 345
Cdd:cd09639 308 RLGRLHRYGEK 318
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
40-371 |
1.72e-09 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 59.52 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 40 DGRDVLGSAPTGTGKTAAFLLPAIQHLldfprKKSGppRVLVVTPTRELAMQVADQAKELCAHNHLDIATITGgvAYMNH 119
Cdd:COG1204 37 EGKNLVVSAPTASGKTLIAELAILKAL-----LNGG--KALYIVPLRALASEKYREFKRDFEELGIKVGVSTG--DYDSD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 120 AEVFSENqDIVVATTGRLLQYIKEENFDCRAVEILILDEA------DRmldmGFanDIETIAgeTRWRK-----QTMLFS 188
Cdd:COG1204 108 DEWLGRY-DILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddeSR----GP--TLEVLL--ARLRRlnpeaQIVALS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 189 ATLEGeaIRDFAERLLEDPIEIDADPSRRERKKIQQ--FHYRADTLEHK---TALLCHLLKQDEvtKAIVFVRKR----- 258
Cdd:COG1204 179 ATIGN--AEEIAEWLDAELVKSDWRPVPLNEGVLYDgvLRFDDGSRRSKdptLALALDLLEEGG--QVLVFVSSRrdaes 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 259 ------------------ERLRELVQWLREAG--IEPCYLE------------GEMPQakrneAVRRLV-----DGQVKV 301
Cdd:COG1204 255 lakkladelkrrltpeerEELEELAEELLEVSeeTHTNEKLadclekgvafhhAGLPS-----ELRRLVedafrEGLIKV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 302 LVATD-------VASRGLDIENVSHVFNFDLPrTADvYLHRIGRTGRAGR--KGTAIsLVEAHDFPLFGKITRYIE---E 369
Cdd:COG1204 330 LVATPtlaagvnLPARRVIIRDTKRGGMVPIP-VLE-FKQMAGRAGRPGYdpYGEAI-LVAKSSDEADELFERYILgepE 406
|
..
gi 1468173135 370 PI 371
Cdd:COG1204 407 PI 408
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
300-358 |
4.55e-09 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 52.71 E-value: 4.55e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1468173135 300 KVLVATDVASRGLDIENVSHVFNFDLPRTADVYLHRIGRTGRAGRKGtaislVEAHDFP 358
Cdd:cd18785 24 EILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE-----GEVILFV 77
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
48-345 |
4.72e-09 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 57.85 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 48 APTGTGKTAAFLLPAiQHLLdfprKKSGPPRVLVVTPTRELAMQVADQAKELCAHNH--LDIATITGGVAYMNHAEVFSE 125
Cdd:TIGR01587 6 APTGYGKTEAALLWA-LHSI----KSQKADRVIIALPTRATINAMYRRAKELFGSELvgLHHSSSFSRIKEMGDSEEFEH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 126 NQDIVVATTGRLLQYI---------------KEENFDCRAVEI----LILDEADRMLDMGFANDIETIAGETRWRKQTML 186
Cdd:TIGR01587 81 LFPLYIHSNDKLFLDPitvctidqvlksvfgEFGHYEFTLASIanslLIFDEVHFYDEYTLALILAVLEVLKDNDVPILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 187 FSATLEgEAIRDFAERLLEDPIEIDADPSRRERKKIQQFHYR-ADTLEHKTALLCHLLKQDEVTKAIVFVRKRERLRELV 265
Cdd:TIGR01587 161 MSATLP-KFLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIeSDKVGEISSLERLLEFIKKGGSIAIIVNTVDRAQEFY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 266 QWLREAGIEPCY--LEGEMPQA----KRNEAVRRLVDGQVK-VLVATDVASRGLDIenvshvfNFDL----PRTADVYLH 334
Cdd:TIGR01587 240 QQLKEKAPEEEIilYHSRFTEKdrakKEAELLREMKKSNEKfVIVATQVIEASLDI-------SADVmiteLAPIDSLIQ 312
|
330
....*....|.
gi 1468173135 335 RIGRTGRAGRK 345
Cdd:TIGR01587 313 RLGRLHRYGRK 323
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
200-352 |
4.73e-09 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 58.73 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 200 AERLLEDPieidadpsrrerkKIQQFHYRADTL--EH-KTALLCHLLKQ----DEVTKAIVFVRKRERLRELVQWLREAG 272
Cdd:PRK13766 323 SKRLVEDP-------------RFRKAVRKAKELdiEHpKLEKLREIVKEqlgkNPDSRIIVFTQYRDTAEKIVDLLEKEG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 273 IEPCYLEGE--------MPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIENVSHVFNFDLPRTADVYLHRIGRTGRaGR 344
Cdd:PRK13766 390 IKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRTGR-QE 468
|
....*...
gi 1468173135 345 KGTAISLV 352
Cdd:PRK13766 469 EGRVVVLI 476
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
40-159 |
1.66e-07 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 51.05 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 40 DGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRkksgpPRVLVVTPTRELAmqvADQAKELCA-----HNHLDIATITGGV 114
Cdd:cd17923 14 AGRSVVVTTGTASGKSLCYQLPILEALLRDPG-----SRALYLYPTKALA---QDQLRSLRElleqlGLGIRVATYDGDT 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1468173135 115 AYMNHAEVFSENQDIVVaTTGRLLQYI------KEENFdCRAVEILILDEA 159
Cdd:cd17923 86 PREERRAIIRNPPRILL-TNPDMLHYAllphhdRWARF-LRNLRYVVLDEA 134
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
49-159 |
2.38e-07 |
|
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: 51.11 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 49 PTGTGKT--AAFLLPAIQHLLDfpRKKSGPPRVLVVTPTRELAMQvadQAKELCAHNHLDIATITGG-VAYMNHAEVFSE 125
Cdd:cd18034 24 PTGSGKTliAVMLIKEMGELNR--KEKNPKKRAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSGEmGVDKWTKERWKE 98
|
90 100 110
....*....|....*....|....*....|....*..
gi 1468173135 126 ---NQDIVVATTGRLLQYIKEENFDCRAVEILILDEA 159
Cdd:cd18034 99 eleKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
48-314 |
3.70e-07 |
|
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: 52.39 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 48 APTGTGKTAAFLLPAIQHlldfpRKKSGPPRVLVVTPTRELAMQVADQAKELcahNHLDIATITGGVAYMNHAEVFSENQ 127
Cdd:COG1203 154 APTGGGKTEAALLFALRL-----AAKHGGRRIIYALPFTSIINQTYDRLRDL---FGEDVLLHHSLADLDLLEEEEEYES 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 128 D--------------IVVATTGRLLQ-YIKEENFDCR-------AVeiLILDEADrMLDmgfANDIETIAGETRWRKQ-- 183
Cdd:COG1203 226 EarwlkllkelwdapVVVTTIDQLFEsLFSNRKGQERrlhnlanSV--IILDEVQ-AYP---PYMLALLLRLLEWLKNlg 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 184 --TMLFSATL---EGEAIRDFAERLLEDPIEIDADPSRRERKKIQqfhYRADTLEHkTALLCHLLKQDEVTKAIVFVR-K 257
Cdd:COG1203 300 gsVILMTATLpplLREELLEAYELIPDEPEELPEYFRAFVRKRVE---LKEGPLSD-EELAELILEALHKGKSVLVIVnT 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1468173135 258 RERLRELVQWLREAG--IEPCYLEGEMPQAKR----NEAVRRLVDGQVKVLVATDVASRGLDI 314
Cdd:COG1203 376 VKDAQELYEALKEKLpdEEVYLLHSRFCPADRseieKEIKERLERGKPCILVSTQVVEAGVDI 438
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
42-162 |
6.24e-07 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 49.34 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 42 RDVLGSAPTGTGKTAAFLLPAiqhLLDFPRKKsgppRVLVVTPTRELAMQVADQAKELCAHNHldIATITGGVaymnhAE 121
Cdd:cd17918 37 MDRLLSGDVGSGKTLVALGAA---LLAYKNGK----QVAILVPTEILAHQHYEEARKFLPFIN--VELVTGGT-----KA 102
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1468173135 122 VFSENQDIVVATTGRLLQYIKEENFDcraveILILDEADRM 162
Cdd:cd17918 103 QILSGISLLVGTHALLHLDVKFKNLD-----LVIVDEQHRF 138
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
251-349 |
9.17e-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: 47.97 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 251 AIVFVRKRERLRELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIENVSHVFNFDLPRTAD 330
Cdd:cd18794 33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112
|
90
....*....|....*....
gi 1468173135 331 VYLHRIGRTGRAGRKGTAI 349
Cdd:cd18794 113 SYYQESGRAGRDGLPSECI 131
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
40-89 |
1.01e-06 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 51.26 E-value: 1.01e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1468173135 40 DGRDVLGSAPTGTGKT-AAFlLPAIQHLLDFPRKKSGPP--RVLVVTPTRELA 89
Cdd:COG1201 38 AGESTLLIAPTGSGKTlAAF-LPALDELARRPRPGELPDglRVLYISPLKALA 89
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
23-346 |
2.17e-06 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 50.10 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 23 GYQRPTAIQAAAIPAAMDGRDVLGSAPTGTGKTAAFLLPAIqhLLDfprkksgpPRVLVVTPTRELaMQvaDQAKELCAH 102
Cdd:PRK11057 22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPAL--VLD--------GLTLVVSPLISL-MK--DQVDQLLAN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 103 nhldiatitgGVA--YMNHAEVFSENQDIVVAT-TGRL-LQYIKEE-----NFDCRAVE----ILILDEADRMLDMGFAN 169
Cdd:PRK11057 89 ----------GVAaaCLNSTQTREQQLEVMAGCrTGQIkLLYIAPErlmmdNFLEHLAHwnpaLLAVDEAHCISQWGHDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 170 DIETIA-GETRWRKQT---MLFSATLEGEAIRDFAERL-LEDP-IEIdadpSRRERKKIQQfhyradTLEHKTALLCHLL 243
Cdd:PRK11057 159 RPEYAAlGQLRQRFPTlpfMALTATADDTTRQDIVRLLgLNDPlIQI----SSFDRPNIRY------TLVEKFKPLDQLM 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 244 K--QDEVTKA-IVFVRKRERLRELVQWLREAGIEPCYLEGEMPQAKRN---EAVRRlvdGQVKVLVATDVASRGLDIENV 317
Cdd:PRK11057 229 RyvQEQRGKSgIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRAdvqEAFQR---DDLQIVVATVAFGMGINKPNV 305
|
330 340
....*....|....*....|....*....
gi 1468173135 318 SHVFNFDLPRTADVYLHrigRTGRAGRKG 346
Cdd:PRK11057 306 RFVVHFDIPRNIESYYQ---ETGRAGRDG 331
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
39-112 |
2.71e-06 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 49.86 E-value: 2.71e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1468173135 39 MDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSGPPRVLVVTPTRELAMQVADQAKELCAHNHLDI--ATITG 112
Cdd:TIGR04121 26 LEGRSGLLIAPTGSGKTLAGFLPSLIDLAGPEAPKEKGLHTLYITPLRALAVDIARNLQAPIEELGLPIrvETRTG 101
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
39-212 |
1.11e-05 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 45.99 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 39 MDGRDVLGSAPTGTGKTAAFLLPAiqHLLDfprkksGPprVLVVTPTRELaMQvaDQAKELCAHNhLDIATITGGVAYMN 118
Cdd:cd17920 25 LAGRDVLVVMPTGGGKSLCYQLPA--LLLD------GV--TLVVSPLISL-MQ--DQVDRLQQLG-IRAAALNSTLSPEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 119 HAEVFSENQD------------IVVATTGRLLQYIKEENFDCRAVeiliLDEA--------D-R--MLDMGfandietIA 175
Cdd:cd17920 91 KREVLLRIKNgqykllyvtperLLSPDFLELLQRLPERKRLALIV----VDEAhcvsqwghDfRpdYLRLG-------RL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1468173135 176 GETRWRKQTMLFSATLEGEAIRDFAERL-LEDPIEIDA 212
Cdd:cd17920 160 RRALPGVPILALTATATPEVREDILKRLgLRNPVIFRA 197
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
256-355 |
1.45e-05 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 45.03 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 256 RKRERLRELVQWLREAgiepcYLEGEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIENVSH--VFNFDLPRTADVYL 333
Cdd:cd18810 40 KLATQLRQLVPEARIA-----IAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTiiIERADKFGLAQLYQ 114
|
90 100
....*....|....*....|..
gi 1468173135 334 HRiGRTGRAGRKGTAISLVEAH 355
Cdd:cd18810 115 LR-GRVGRSKERAYAYFLYPDQ 135
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
47-161 |
1.61e-05 |
|
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: 44.86 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 47 SAPTGTGKT--AAFLlpaIQHLLdfprKKSGPPRVLVVTPTRELAMQVADQAKelcahNHLDIATItgGVAYMNHAEVFS 124
Cdd:cd18032 26 VMATGTGKTytAAFL---IKRLL----EANRKKRILFLAHREELLEQAERSFK-----EVLPDGSF--GNLKGGKKKPDD 91
|
90 100 110
....*....|....*....|....*....|....*..
gi 1468173135 125 EnqDIVVATTGRLLQYIKEENFDCRAVEILILDEADR 161
Cdd:cd18032 92 A--RVVFATVQTLNKRKRLEKFPPDYFDLIIIDEAHH 126
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
48-161 |
6.03e-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: 43.66 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 48 APTGTGKTAAFLLPAIQHLldfpRKKSGppRVLVVTPTRELAMQVADQAKELCaHNHLDIATITGGVAYMNHAEVFSENQ 127
Cdd:cd18035 23 LPTGLGKTIIAILVAADRL----TKKGG--KVLILAPSRPLVEQHAENLKRVL-NIPDKITSLTGEVKPEERAERWDASK 95
|
90 100 110
....*....|....*....|....*....|....
gi 1468173135 128 dIVVATTGRLLQYIKEENFDCRAVEILILDEADR 161
Cdd:cd18035 96 -IIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
44-159 |
6.31e-05 |
|
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438707 [Multi-domain] Cd Length: 159 Bit Score: 43.22 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 44 VLGSAPTGTGKTAafLLPaiQHLLDFPRKKSGPPRVLVVTPTRELAMQVADQ-AKELCahnhldiATITGGVAYMNHAE- 121
Cdd:cd17917 4 VVIVGETGSGKTT--QVP--QFLLEDGLAKGGKGRIVCTQPRRIAAISVAERvAEERG-------EKLGEEVGYQIRFEs 72
|
90 100 110
....*....|....*....|....*....|....*...
gi 1468173135 122 VFSENQDIVVATTGRLLQYIkEENFDCRAVEILILDEA 159
Cdd:cd17917 73 KTSSKTRIKFCTDGILLREL-LSDPLLSGYSHVILDEA 109
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
42-133 |
7.75e-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: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 42 RDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSGPPRVLVVTPTRELAMQVADQAKELCAHNHLDIATITGGVAYMNHAE 121
Cdd:cd18023 18 KNFVVSAPTGSGKTVLFELAILRLLKERNPLPWGNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSCAELTGDTEMDDTFE 97
|
90
....*....|..
gi 1468173135 122 VFseNQDIVVAT 133
Cdd:cd18023 98 IQ--DADIILTT 107
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
47-159 |
1.16e-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: 42.29 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 47 SAPTGTGKTaAFLLPAIQHLldfprkksGPPRVLVVTPTRELAMQVADQAKELCAHNHLDIatITGGvaymnhAEVFSEN 126
Cdd:cd17926 24 VLPTGSGKT-LTALALIAYL--------KELRTLIVVPTDALLDQWKERFEDFLGDSSIGL--IGGG------KKKDFDD 86
|
90 100 110
....*....|....*....|....*....|...
gi 1468173135 127 QDIVVATTGRLLQYIKEENFDCRAVEILILDEA 159
Cdd:cd17926 87 ANVVVATYQSLSNLAEEEKDLFDQFGLLIVDEA 119
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
39-161 |
1.23e-04 |
|
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: 42.80 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 39 MDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSGppRVLVVTPTRELAMQVADQAKELCAHNHLDIATITGGVAYMN 118
Cdd:cd17927 15 LKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKG--KVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENV 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1468173135 119 HAEVFSENQDIVVATTGRLLQYIKE-ENFDCRAVEILILDEADR 161
Cdd:cd17927 93 SVEQIVESSDVIIVTPQILVNDLKSgTIVSLSDFSLLVFDECHN 136
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
48-159 |
1.90e-04 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 42.28 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 48 APTGTGKTAAFLLPAIQHlldfpRKKSGPPRVLVVTPTRELAMQVADQAKELCAHN---------HLDIATITGGVAYMN 118
Cdd:cd17930 8 APTGSGKTEAALLWALKL-----AARGGKRRIIYALPTRATINQMYERIREILGRLddedkvlllHSKAALELLESDEEP 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1468173135 119 HAEVFSENQD-----------IVVATTGRLLQ-YIKEENFDCRAVEI----LILDEA 159
Cdd:cd17930 83 DDDPVEAVDWalllkrswlapIVVTTIDQLLEsLLKYKHFERRLHGLansvVVLDEV 139
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
241-351 |
2.21e-04 |
|
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: 41.48 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 241 HLLKQDEVTKAIVFVRKRERLRELVQWLREAGIEPCYLE------GEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDI 314
Cdd:cd18796 31 VIFLLERHKSTLVFTNTRSQAERLAQRLRELCPDRVPPDfialhhGSLSRELREEVEAALKRGDLKVVVATSSLELGIDI 110
|
90 100 110
....*....|....*....|....*....|....*..
gi 1468173135 315 ENVSHVFNFDLPRTADVYLHRIgrtGRAGRKGTAISL 351
Cdd:cd18796 111 GDVDLVIQIGSPKSVARLLQRL---GRSGHRPGAASK 144
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
48-161 |
2.38e-04 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 41.50 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 48 APTGTGKT--AAFLlpaIQHLldfpRKKSGPPRVLVVTPTRELamqvADQAKE---LCAHNHLDIATITGGvaymNHAEV 122
Cdd:pfam04851 30 MATGSGKTltAAKL---IARL----FKKGPIKKVLFLVPRKDL----LEQALEefkKFLPNYVEIGEIISG----DKKDE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1468173135 123 FSENQDIVVATTGRL-------LQYIKEENFDCraveiLILDEADR 161
Cdd:pfam04851 95 SVDDNKIVVTTIQSLykalelaSLELLPDFFDV-----IIIDEAHR 135
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
40-86 |
3.02e-04 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 42.99 E-value: 3.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1468173135 40 DGRDVLGSAPTGTGKTAAFLLPAIQHLLDfpRKKsgppRVLVVTPTR 86
Cdd:COG1199 32 EGRHLLIEAGTGTGKTLAYLVPALLAARE--TGK----KVVISTATK 72
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
209-346 |
4.13e-04 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 40.70 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 209 EIDADPSRRERKKIqqfhyrADTLEHKTALLCHLLKQDE-VTKAIVFVRKRERLRELVQWLREAGIEpcyleGEMPQAKR 287
Cdd:cd18789 15 EYLGLGAHRKRRLL------AAMNPNKLRALEELLKRHEqGDKIIVFTDNVEALYRYAKRLLKPFIT-----GETPQSER 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1468173135 288 NEAVRRLVDGQVKVLVATDVASRGldienvshvfnFDLPrTADV-------------YLHRIGRTGRAGRKG 346
Cdd:cd18789 84 EEILQNFREGEYNTLVVSKVGDEG-----------IDLP-EANVaiqisghggsrrqEAQRLGRILRPKKGG 143
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
250-338 |
4.47e-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: 39.85 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 250 KAIVFVRKRERLRELVQWLREAGIEPCYLEGEMPQAKRN-EAVRRLVDGQVK--VLVATDVASRGLDIENVSHVFnFDLP 326
Cdd:cd18799 8 KTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdEALILLFFGELKppILVTVDLLTTGVDIPEVDNVV-FLRP 86
|
90
....*....|...
gi 1468173135 327 -RTADVYLHRIGR 338
Cdd:cd18799 87 tESRTLFLQMLGR 99
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
39-133 |
7.83e-04 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I 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: 350831 [Multi-domain] Cd Length: 202 Bit Score: 40.57 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 39 MDGRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRKKSGppRVLVvtptreLAMQV---ADQAKELCAH---NHLDIATITG 112
Cdd:cd18073 15 MKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKG--KVVF------FATKVpvyEQQKSVFSKYferHGYRVTGISG 86
|
90 100
....*....|....*....|.
gi 1468173135 113 GVAYMNHAEVFSENQDIVVAT 133
Cdd:cd18073 87 ATAENVPVEQIIENNDIIILT 107
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
238-353 |
9.14e-04 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 39.94 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 238 LLCHLLKQDEVTKAIVFVRKRERLRELVQWLREAgiepcYLEGEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIENV 317
Cdd:cd18792 31 YVYPRIEESEKLDLKSIEALAEELKELVPEARVA-----LLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNA 105
|
90 100 110
....*....|....*....|....*....|....*..
gi 1468173135 318 SHVFNFDLPRTADVYLHRI-GRTGRAGRKGTAISLVE 353
Cdd:cd18792 106 NTMIIEDADRFGLSQLHQLrGRVGRGKHQSYCYLLYP 142
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
48-341 |
2.19e-03 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 40.24 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 48 APTGTGKTAaFLLPAIQHLLdfprKKSGppRVLVVTPTRELAMQVADQAKElcAHNHLDIATITGGvaymnhaevfSENQ 127
Cdd:COG4098 136 AVCGAGKTE-MLFPAIAEAL----KQGG--RVCIATPRVDVVLELAPRLQQ--AFPGVDIAALYGG----------SEEK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 128 ----DIVVATTGRLLQYikEENFDCraveiLILDEADRmldMGFANDIETIAGETRWRKQTmlfsATLegeairdfaerl 203
Cdd:COG4098 197 yryaQLVIATTHQLLRF--YQAFDL-----LIIDEVDA---FPYSGDPMLQYAVKRARKPD----GKL------------ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 204 ledpIEIDADPSRRERKKIQQ-----------FHYRA----------------------DTLEHktaLLCHLLKQDEvtK 250
Cdd:COG4098 251 ----IYLTATPSKALQRQVKRgklkvvklparYHGHPlpvpkfkwlgnwkkrlrrgklpRKLLK---WLKKRLKEGR--Q 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 251 AIVFVRKRERLRELVQWLRE--AGIEPCYLEGEMPQakRNEAVRRLVDGQVKVLVATDVASRGLDIENVsHVFNFDlprt 328
Cdd:COG4098 322 LLIFVPTIELLEQLVALLQKlfPEERIAGVHAEDPE--RKEKVQAFRDGEIPILVTTTILERGVTFPNV-DVAVLG---- 394
|
330 340
....*....|....*....|...
gi 1468173135 329 ADvylHRI----------GRTGR 341
Cdd:COG4098 395 AD---HPVfteaalvqiaGRVGR 414
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
263-341 |
3.28e-03 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 38.38 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 263 ELVQWLREAGIEPCYLEGEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIENVSHVFNFD-----LPRTADVYLHRIG 337
Cdd:cd18790 42 DLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegFLRSETSLIQTIG 121
|
....
gi 1468173135 338 RTGR 341
Cdd:cd18790 122 RAAR 125
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
198-344 |
4.47e-03 |
|
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350178 [Multi-domain] Cd Length: 171 Bit Score: 37.90 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 198 DFAERLLEDPIEIDADPSRRERKKIQQFHYRadtlEHKTALLCHLLKQDEVTKAivfvrkRERLRELVQWLREAGIEPCY 277
Cdd:cd18791 10 DILELLGISSEKEDPDYVDAAVRLILQIHRT----EEPGDILVFLPGQEEIERL------CELLREELLSPDLGKLLVLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 278 LEGEMPQAKRNEAVRRLVDGQVKVLVATDVASRGLDIENVSHVFNFDLPRTAdVYLHRIG----------------RTGR 341
Cdd:cd18791 80 LHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEK-VYDPRTGlsslvtvwiskasaeqRAGR 158
|
...
gi 1468173135 342 AGR 344
Cdd:cd18791 159 AGR 161
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
47-99 |
5.33e-03 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 38.08 E-value: 5.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1468173135 47 SAPTGTGKTAAFLLPAIqhlldFPRKKSGppRVLVVTPTRELAMQVADQAKEL 99
Cdd:cd17924 38 IAPTGVGKTTFGLATSL-----YLASKGK--RSYLIFPTKSLVKQAYERLSKY 83
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
41-208 |
7.46e-03 |
|
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438711 [Multi-domain] Cd Length: 174 Bit Score: 37.31 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 41 GRDVLGSAPTGTGKTAAFLLPAIQHLLDFPRkksgppRVLVVTPTRELAMQVADQAKElcahnhLDIATITGGVAYMNHA 120
Cdd:cd17990 17 GGQVVLEAPPGAGKTTRVPLALLAELWIAGG------KIIVLEPRRVAARAAARRLAT------LLGEAPGETVGYRVRG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468173135 121 E-VFSENQDIVVATTGRLLQYIkEENFDCRAVEILILDEA-DRML--DMGFANDIEtIAGETRWRKQTMLFSATLEGEAi 196
Cdd:cd17990 85 EsRVGRRTRVEVVTEGVLLRRL-QRDPELSGVGAVILDEFhERSLdaDLALALLLE-VQQLLRDDLRLLAMSATLDGDG- 161
|
170
....*....|..
gi 1468173135 197 rdFAERLLEDPI 208
Cdd:cd17990 162 --LAALLPEAPV 171
|
|
| |
