|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
1-460 |
0e+00 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 899.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 1 MSTTSFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQALVLCP 80
Cdd:PRK11776 1 MSMTAFSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 81 TRELADQVSKELRRLARFTQNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRML 160
Cdd:PRK11776 81 TRELADQVAKEIRRLARFIPNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 161 DMGFTDAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNVEVDDGDEAPAIEQVFFETTREKRLPLLISVLSHY 240
Cdd:PRK11776 161 DMGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDERLPALQRLLLHH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 241 QPASCVVFCNTKKDCQSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRSCRVLVATDVAARGLDIKDLELVVNFELA 320
Cdd:PRK11776 241 QPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 321 FDPEVHVHRIGRTGRAGMSGLAVSLCTPQEMTRAHAIEDYLQMKLKWTPAEQVSRSANTMLEPEMVTLCIDGGRKAKIRP 400
Cdd:PRK11776 321 RDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEPLPSLSPLSGVPLLPEMVTLCIDGGKKDKLRP 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 401 GDILGALTGEASLTAADVGKIDMFPVHAYVAIRKASAKRALQQLQQGKIKGKNCKARLLK 460
Cdd:PRK11776 401 GDILGALTGDAGLDGAQIGKINVTDFHAYVAVERAVAKKALKKLQNGKIKGKSFRVRLLK 460
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
3-367 |
0e+00 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 531.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 3 TTSFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVG-EFVTQALVLCPT 81
Cdd:COG0513 1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSrPRAPQALILAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 82 RELADQVSKELRRLARFTqNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLD 161
Cdd:COG0513 81 RELALQVAEELRKLAKYL-GLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 162 MGFTDAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNVEVDDGDE-APAIEQVFFETTREKRLPLLISVLSHY 240
Cdd:COG0513 160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENAtAETIEQRYYLVDKRDKLELLRRLLRDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 241 QPASCVVFCNTKKDCQSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRSCRVLVATDVAARGLDIKDLELVVNFELA 320
Cdd:COG0513 240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 933675871 321 FDPEVHVHRIGRTGRAGMSGLAVSLCTPQEMTRAHAIEDYLQMKLKW 367
Cdd:COG0513 320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEE 366
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
4-343 |
2.87e-91 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 289.44 E-value: 2.87e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 4 TSFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQALVLCPTRE 83
Cdd:PRK11634 6 TTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELKAPQILVLAPTRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 84 LADQVSKELRRLARFTQNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMG 163
Cdd:PRK11634 86 LAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 164 FTDAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNVEVDDG-DEAPAIEQVFFETTREKRLPLLISVLSHYQP 242
Cdd:PRK11634 166 FIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSvTTRPDISQSYWTVWGMRKNEALVRFLEAEDF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 243 ASCVVFCNTKKDCQSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRSCRVLVATDVAARGLDIKDLELVVNFELAFD 322
Cdd:PRK11634 246 DAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMD 325
|
330 340
....*....|....*....|.
gi 933675871 323 PEVHVHRIGRTGRAGMSGLAV 343
Cdd:PRK11634 326 SESYVHRIGRTGRAGRAGRAL 346
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
16-207 |
3.84e-90 |
|
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: 272.39 E-value: 3.84e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 16 LSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFV----TQALVLCPTRELADQVSKE 91
Cdd:cd00268 2 LKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKkgrgPQALVLAPTRELAMQIAEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 92 LRRLARFTqNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMGFTDAIDDV 171
Cdd:cd00268 82 ARKLGKGT-GLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 933675871 172 IAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNVE 207
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
4-366 |
1.00e-87 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 274.51 E-value: 1.00e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 4 TSFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIG----LLDKIAVGEFVTQALVLC 79
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPalqhLLDFPRRKSGPPRILILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 80 PTRELADQVSKELRRLARFTqNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRM 159
Cdd:PRK11192 81 PTRELAMQVADQARELAKHT-HLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 160 LDMGFTDAIDDVIAYTPPQRQTLLFSATYP-AGIEQISARVQRQPVNVEVDDG-DEAPAIEQ-VFFETTREKRLPLLISV 236
Cdd:PRK11192 160 LDMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSrRERKKIHQwYYRADDLEHKTALLCHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 237 LSHYQPASCVVFCNTKKDCQSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRSCRVLVATDVAARGLDIKDLELVVN 316
Cdd:PRK11192 240 LKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVIN 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 933675871 317 FELAFDPEVHVHRIGRTGRAGMSGLAVSLCTPQEMTRAHAIEDYLQMKLK 366
Cdd:PRK11192 320 FDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLK 369
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
5-362 |
2.90e-79 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 253.58 E-value: 2.90e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 5 SFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKI------AVGEFVTQALVL 78
Cdd:PRK10590 2 SFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLitrqphAKGRRPVRALIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 79 CPTRELADQVSKELRRLARFTqNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADR 158
Cdd:PRK10590 82 TPTRELAAQIGENVRDYSKYL-NIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 159 MLDMGFTDAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNVEVDDGDEAP-AIEQ-VFFETTREKR--LPLLI 234
Cdd:PRK10590 161 MLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASeQVTQhVHFVDKKRKRelLSQMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 235 SVLSHYQpasCVVFCNTKKDCQSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRSCRVLVATDVAARGLDIKDLELV 314
Cdd:PRK10590 241 GKGNWQQ---VLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHV 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 933675871 315 VNFELAFDPEVHVHRIGRTGRAGMSGLAVSLCTPQEMTRAHAIEDYLQ 362
Cdd:PRK10590 318 VNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLK 365
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
1-362 |
1.31e-77 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 247.96 E-value: 1.31e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 1 MSTTSFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIG-----LLDKIAVGEFVTQ- 74
Cdd:PRK04837 5 LTEQKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTAtfhylLSHPAPEDRKVNQp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 75 -ALVLCPTRELADQVSKELRRLARFTqNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVL 153
Cdd:PRK04837 85 rALIMAPTRELAVQIHADAEPLAQAT-GLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 154 DEADRMLDMGFtdaIDDvIAY------TPPQRQTLLFSATypagieqISARVQR-------QPVNVEVddgdeAPAI--- 217
Cdd:PRK04837 164 DEADRMFDLGF---IKD-IRWlfrrmpPANQRLNMLFSAT-------LSYRVRElafehmnNPEYVEV-----EPEQktg 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 218 ----EQVFFETTREKrLPLLISVLSHYQPASCVVFCNTKKDCQSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRSC 293
Cdd:PRK04837 228 hrikEELFYPSNEEK-MRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDL 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 933675871 294 RVLVATDVAARGLDIKDLELVVNFELAFDPEVHVHRIGRTGRAGMSGLAVSLCTPQEMTRAHAIEDYLQ 362
Cdd:PRK04837 307 DILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIG 375
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
3-366 |
2.12e-76 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 246.36 E-value: 2.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 3 TTSFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIA---------VGEfvT 73
Cdd:PRK01297 86 KTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLqtpppkeryMGE--P 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 74 QALVLCPTRELADQVSKELRRLARFTqNIKILTLCGGQPMGHQLDSLvHAPH--IVVGTPGRIQEHLRKKTLVLDDLKIL 151
Cdd:PRK01297 164 RALIIAPTRELVVQIAKDAAALTKYT-GLNVMTFVGGMDFDKQLKQL-EARFcdILVATPGRLLDFNQRGEVHLDMVEVM 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 152 VLDEADRMLDMGFTDAIDDVIAYTPP--QRQTLLFSATYPAGIEQISARVQRQPVNVEVDDGDEAPA-IEQVFFETTREK 228
Cdd:PRK01297 242 VLDEADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDtVEQHVYAVAGSD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 229 RLPLLISVLSHYQPASCVVFCNTKKDCQSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRSCRVLVATDVAARGLDI 308
Cdd:PRK01297 322 KYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHI 401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 933675871 309 KDLELVVNFELAFDPEVHVHRIGRTGRAGMSGLAVSLCTPQEMTRAHAIEDYLQMKLK 366
Cdd:PRK01297 402 DGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKIS 459
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
5-371 |
3.21e-75 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 241.27 E-value: 3.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 5 SFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQALVLCPTREL 84
Cdd:PTZ00424 29 SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDLNACQALILAPTREL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 85 ADQVSKELRRLARFTQnIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMGF 164
Cdd:PTZ00424 109 AQQIQKVVLALGDYLK-VRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 165 TDAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNVEVDDgDEAP--AIEQVFFETTREK-RLPLLISVLSHYQ 241
Cdd:PTZ00424 188 KGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKK-DELTleGIRQFYVAVEKEEwKFDTLCDLYETLT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 242 PASCVVFCNTKKDCQSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRSCRVLVATDVAARGLDIKDLELVVNFELAF 321
Cdd:PTZ00424 267 ITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPA 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 933675871 322 DPEVHVHRIGRTGRAGMSGLAVSLCTPQEMTRAHAIEDYLQMKLKWTPAE 371
Cdd:PTZ00424 347 SPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPME 396
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
4-348 |
4.52e-72 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 236.98 E-value: 4.52e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 4 TSFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFgigLLDkiAVGEFVTQA-------- 75
Cdd:PTZ00110 130 VSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAF---LLP--AIVHINAQPllrygdgp 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 76 --LVLCPTRELADQVSKELRRlarFTQNIKILTLC--GGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKIL 151
Cdd:PTZ00110 205 ivLVLAPTRELAEQIREQCNK---FGASSKIRNTVayGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVTNLRRVTYL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 152 VLDEADRMLDMGFTDAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQR-QPVNVEVDDGD--EAPAIEQ-VFFETTRE 227
Cdd:PTZ00110 282 VLDEADRMLDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKeEPVHVNVGSLDltACHNIKQeVFVVEEHE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 228 KRLPLLISVLSHYQPASCV-VFCNTKKDCQSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRSCRVLVATDVAARGL 306
Cdd:PTZ00110 362 KRGKLKMLLQRIMRDGDKIlIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGL 441
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 933675871 307 DIKDLELVVNFELAFDPEVHVHRIGRTGRAGMSGLAVSLCTP 348
Cdd:PTZ00110 442 DVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTP 483
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
1-411 |
7.51e-68 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 226.76 E-value: 7.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 1 MSTTSFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVT------- 73
Cdd:PRK04537 6 LTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSRPALAdrkpedp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 74 QALVLCPTRELADQVSKELrrlARFTQNI--KILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLV-LDDLKI 150
Cdd:PRK04537 86 RALILAPTRELAIQIHKDA---VKFGADLglRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVsLHACEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 151 LVLDEADRMLDMGFTDAIDDVIAYTPPQ--RQTLLFSATYPAGIEQISARVQRQP--VNVEVDDGDEAPAIEQVFFETTR 226
Cdd:PRK04537 163 CVLDEADRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPekLVVETETITAARVRQRIYFPADE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 227 EKrLPLLISVLSHYQPASCVVFCNTKKDCQSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRSCRVLVATDVAARGL 306
Cdd:PRK04537 243 EK-QTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 307 DIKDLELVVNFELAFDPEVHVHRIGRTGRAGMSGLAVSLCTPQEMTRAHAIEDYLQMKLkwtPAEQVSRSANTML-EPEM 385
Cdd:PRK04537 322 HIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKI---PVEPVTAELLTPLpRPPR 398
|
410 420
....*....|....*....|....*.
gi 933675871 386 VTLcidGGRKAKIRPGDILGALTGEA 411
Cdd:PRK04537 399 VPV---EGEEADDEAGDSVGTIFREA 421
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
16-206 |
8.11e-59 |
|
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: 191.70 E-value: 8.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 16 LSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKI---AVGEFVTQALVLCPTRELADQVSKEL 92
Cdd:cd17947 2 LRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyrPKKKAATRVLVLVPTRELAMQCFSVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 93 RRLARFTqNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRK-KTLVLDDLKILVLDEADRMLDMGFTDAIDDV 171
Cdd:cd17947 82 QQLAQFT-DITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNsPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 933675871 172 IAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNV 206
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
5-198 |
3.36e-57 |
|
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: 188.46 E-value: 3.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 5 SFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGI----GLLDKIAVGEFVT------Q 74
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLpiisKLLEDGPPSVGRGrrkaypS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 75 ALVLCPTRELADQVSKELRRLARFTQnIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLD 154
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSG-VRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIKFLVLD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 933675871 155 EADRMLDMGFTDAIDDVIAYT--PP--QRQTLLFSATYPAGIEQISAR 198
Cdd:cd17967 160 EADRMLDMGFEPQIRKIVEHPdmPPkgERQTLMFSATFPREIQRLAAD 207
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
6-206 |
9.43e-57 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 186.35 E-value: 9.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 6 FSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQALVLCPTRELA 85
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 86 DQVSKELRRLARFTqNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMGFT 165
Cdd:cd17940 81 LQTSQVCKELGKHM-GVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 933675871 166 DAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNV 206
Cdd:cd17940 160 PIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
28-195 |
1.65e-56 |
|
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: 184.37 E-value: 1.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 28 TPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQALVLCPTRELADQVSKELRRLARFTqNIKILTL 107
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGL-GLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 108 CGGQPMGHQLDSLVHaPHIVVGTPGRIQEHLRKKTLvLDDLKILVLDEADRMLDMGFTDAIDDVIAYTPPQRQTLLFSAT 187
Cdd:pfam00270 80 LGGDSRKEQLEKLKG-PDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157
|
....*...
gi 933675871 188 YPAGIEQI 195
Cdd:pfam00270 158 LPRNLEDL 165
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
6-204 |
2.71e-55 |
|
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: 182.81 E-value: 2.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 6 FSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQALVLCPTRELA 85
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 86 DQVSKELRRLARFTqNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLR---KKTLVLDDLKILVLDEADRMLDM 162
Cdd:cd17955 81 YQIAEQFRALGAPL-GLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSRVKFLVLDEADRLLTG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 933675871 163 GFTDAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPV 204
Cdd:cd17955 160 SFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPF 201
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
19-195 |
3.51e-55 |
|
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: 182.78 E-value: 3.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 19 LNELGYTEMTPVQAAALPAIL-NGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQ-----ALVLCPTRELADQVSKEL 92
Cdd:cd17964 9 LTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRrsgvsALIISPTRELALQIAAEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 93 RRLARFTQNIKILTLCGGQPMGHQLDSLVH-APHIVVGTPGRIQEHLRKKTL--VLDDLKILVLDEADRMLDMGFTDAID 169
Cdd:cd17964 89 KKLLQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVakAFTDLDYLVLDEADRLLDMGFRPDLE 168
|
170 180 190
....*....|....*....|....*....|
gi 933675871 170 DVIAYTPP----QRQTLLFSATYPAGIEQI 195
Cdd:cd17964 169 QILRHLPEknadPRQTLLFSATVPDEVQQI 198
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
217-346 |
1.28e-53 |
|
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: 175.77 E-value: 1.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 217 IEQVFFET-TREKRLPLLISVLSHYQPASCVVFCNTKKDCQSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRSCRV 295
Cdd:cd18787 1 IKQLYVVVeEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 933675871 296 LVATDVAARGLDIKDLELVVNFELAFDPEVHVHRIGRTGRAGMSGLAVSLC 346
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
4-197 |
7.03e-53 |
|
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: 178.62 E-value: 7.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 4 TSFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDK-----IAVGEFVT----Q 74
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGmmkegLTASSFSEvqepQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 75 ALVLCPTRELADQVSKELRRLARFTQnIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLD 154
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTC-IRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILD 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 933675871 155 EADRMLDMGFTDAIDDVIAY--TPP--QRQTLLFSATYPAGIEQISA 197
Cdd:cd18052 202 EADRMLDMGFGPEIRKLVSEpgMPSkeDRQTLMFSATFPEEIQRLAA 248
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
5-189 |
4.88e-52 |
|
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: 174.42 E-value: 4.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 5 SFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVT--QALVLCPTR 82
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVgaRALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 83 ELADQVSKELRRLARFTqNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDM 162
Cdd:cd17959 82 ELALQTLKVTKELGKFT-DLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEM 160
|
170 180
....*....|....*....|....*..
gi 933675871 163 GFTDAIDDVIAYTPPQRQTLLFSATYP 189
Cdd:cd17959 161 GFAEQLHEILSRLPENRQTLLFSATLP 187
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
23-206 |
8.50e-52 |
|
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: 173.66 E-value: 8.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 23 GYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQALVLCPTRELADQVSKELRRLARFTqNI 102
Cdd:cd17939 16 GFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQIQKVVKALGDYM-GV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 103 KILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMGFTDAIDDVIAYTPPQRQTL 182
Cdd:cd17939 95 KVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPPETQVV 174
|
170 180
....*....|....*....|....
gi 933675871 183 LFSATYPAGIEQISARVQRQPVNV 206
Cdd:cd17939 175 LFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
5-207 |
2.82e-51 |
|
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: 172.12 E-value: 2.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 5 SFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQALVLCPTREL 84
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 85 ADQVSKELRRLARfTQNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHL-RKKTLVLDDLKILVLDEADRMLDMG 163
Cdd:cd17954 81 AQQISEQFEALGS-SIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLeNTKGFSLKSLKFLVMDEADRLLNMD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 933675871 164 FTDAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNVE 207
Cdd:cd17954 160 FEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
16-206 |
6.06e-51 |
|
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: 171.22 E-value: 6.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 16 LSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQ-----ALVLCPTRELADQVSK 90
Cdd:cd17960 2 LDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLKRKANLKkgqvgALIISPTRELATQIYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 91 ELRRLARFTQN-IKILTLCGGQPMGHQLDSLV-HAPHIVVGTPGRIQEHLRKKTLVLD--DLKILVLDEADRMLDMGFTD 166
Cdd:cd17960 82 VLQSFLEHHLPkLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSRKADKVKvkSLEVLVLDEADRLLDLGFEA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 933675871 167 AIDDVIAYTPPQRQTLLFSATYPAGIEQIsARVQ-RQPVNV 206
Cdd:cd17960 162 DLNRILSKLPKQRRTGLFSATQTDAVEEL-IKAGlRNPVRV 201
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
5-343 |
7.54e-51 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 179.98 E-value: 7.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 5 SFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLD---KIAVGEFVTQ----ALV 77
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrccTIRSGHPSEQrnplAMV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 78 LCPTRELADQVSKELRRLARFTQnIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEAD 157
Cdd:PLN00206 202 LTPTRELCVQVEDQAKVLGKGLP-FKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVD 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 158 RMLDMGFTDAIDDvIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNVEV-DDGDEAPAIEQ--VFFETTREK-RLPLL 233
Cdd:PLN00206 281 CMLERGFRDQVMQ-IFQALSQPQVLLFSATVSPEVEKFASSLAKDIILISIgNPNRPNKAVKQlaIWVETKQKKqKLFDI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 234 ISVLSHYQPAScVVFCNTKKDCQSVYEALE-SRGISVLALHGDLEQRDRDQVLVRFANRSCRVLVATDVAARGLDIKDLE 312
Cdd:PLN00206 360 LKSKQHFKPPA-VVFVSSRLGADLLANAITvVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVR 438
|
330 340 350
....*....|....*....|....*....|.
gi 933675871 313 LVVNFELAFDPEVHVHRIGRTGRAGMSGLAV 343
Cdd:PLN00206 439 QVIIFDMPNTIKEYIHQIGRASRMGEKGTAI 469
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
16-208 |
5.85e-49 |
|
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: 165.93 E-value: 5.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 16 LSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQ----ALVLCPTRELADQVSKE 91
Cdd:cd17941 2 LKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEdglgALIISPTRELAMQIFEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 92 LRRLARFTqNIKILTLCGGQPMGHQLDSlVHAPHIVVGTPGRIQEHLRKK-TLVLDDLKILVLDEADRMLDMGFTDAIDD 170
Cdd:cd17941 82 LRKVGKYH-SFSAGLIIGGKDVKEEKER-INRMNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEADRILDMGFKETLDA 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 933675871 171 VIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNVEV 208
Cdd:cd17941 160 IVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
21-206 |
1.31e-48 |
|
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: 165.96 E-value: 1.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 21 ELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIA--------VGEFVTQALVLCPTRELADQVSKEL 92
Cdd:cd17945 7 KLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISrlppldeeTKDDGPYALILAPTRELAQQIEEET 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 93 RRLARFtQNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMGFTDAIDDVI 172
Cdd:cd17945 87 QKFAKP-LGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVTKIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 933675871 173 AYTPPQ--------------------RQTLLFSATYPAGIEQISARVQRQPVNV 206
Cdd:cd17945 166 DAMPVSnkkpdteeaeklaasgkhryRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
19-211 |
5.75e-48 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 163.43 E-value: 5.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 19 LNELGYTEMTPVQAAALPAILNG-QDVRAKAKTGSGKTAAFGIGLLDKIAvGEFVTQALVLCPTRELADQVSKELRRLAR 97
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALK-RGKGGRVLVLVPTRELAEQWAEELKKLGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 98 FTqNIKILTLCGGQPMGHQLDSLVH-APHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMGFTDAIDDVIAYTP 176
Cdd:smart00487 80 SL-GLKVVGLYGGDSKREQLRKLESgKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLP 158
|
170 180 190
....*....|....*....|....*....|....*
gi 933675871 177 PQRQTLLFSATYPAGIEQISARVQRQPVNVEVDDG 211
Cdd:smart00487 159 KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFT 193
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
16-208 |
9.57e-48 |
|
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: 162.76 E-value: 9.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 16 LSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAV--GEFVTQALVLCPTRELADQVSKELR 93
Cdd:cd17957 2 LNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKprKKKGLRALILAPTRELASQIYRELL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 94 RLARFTqNIKILTLCGGQpMGHQLDSLVHAPH--IVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMGFTDAIDDV 171
Cdd:cd17957 82 KLSKGT-GLRIVLLSKSL-EAKAKDGPKSITKydILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEI 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 933675871 172 I-AYTPPQRQTLLFSATYPAGIEQISARVQRQPVNVEV 208
Cdd:cd17957 160 LaACTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
16-204 |
1.56e-47 |
|
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: 162.37 E-value: 1.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 16 LSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKI------AVGEFVTQALVLCPTRELADQVS 89
Cdd:cd17961 6 LKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaeSGEEQGTRALILVPTRELAQQVS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 90 KELRRLARF-TQNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVL-DDLKILVLDEADRMLDMGFTDA 167
Cdd:cd17961 86 KVLEQLTAYcRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLlSTLKYLVIDEADLVLSYGYEED 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 933675871 168 IDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPV 204
Cdd:cd17961 166 LKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
4-206 |
1.58e-47 |
|
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: 162.93 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 4 TSFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQ-----ALVL 78
Cdd:cd17953 12 QKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKPgegpiGLIM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 79 CPTRELADQVSKELRRlarFTQNIKILTLC--GGQPMGHQLDSLVHAPHIVVGTPGRIQEHL---RKKTLVLDDLKILVL 153
Cdd:cd17953 92 APTRELALQIYVECKK---FSKALGLRVVCvyGGSGISEQIAELKRGAEIVVCTPGRMIDILtanNGRVTNLRRVTYVVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 933675871 154 DEADRMLDMGFTDAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNV 206
Cdd:cd17953 169 DEADRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
16-206 |
6.76e-46 |
|
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350720 [Multi-domain] Cd Length: 193 Bit Score: 157.71 E-value: 6.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 16 LSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQALVLCPTRELADQVSKELRRL 95
Cdd:cd17962 2 SSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 96 ARFTQNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMGFTDAIDDVIAYT 175
Cdd:cd17962 82 MKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENI 161
|
170 180 190
....*....|....*....|....*....|.
gi 933675871 176 PPQRQTLLFSATYPAGIEQISARVQRQPVNV 206
Cdd:cd17962 162 SHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
16-206 |
6.92e-45 |
|
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: 155.27 E-value: 6.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 16 LSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQ-----ALVLCPTRELADQVSK 90
Cdd:cd17952 2 LNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEKgegpiAVIVAPTRELAQQIYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 91 ELRRLARFTqNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMGFTDAIDD 170
Cdd:cd17952 82 EAKKFGKAY-NLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRS 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 933675871 171 VIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNV 206
Cdd:cd17952 161 IVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
4-198 |
1.53e-44 |
|
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: 155.97 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 4 TSFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKI---AVGEFVTQ------ 74
Cdd:cd18051 21 ETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqGPGESLPSesgyyg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 75 -------ALVLCPTRELADQVSKELRRLArFTQNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDD 147
Cdd:cd18051 101 rrkqyplALVLAPTRELASQIYDEARKFA-YRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGKIGLDY 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 933675871 148 LKILVLDEADRMLDMGFTDAIDDVIAY--TPP--QRQTLLFSATYPAGIeQISAR 198
Cdd:cd18051 180 CKYLVLDEADRMLDMGFEPQIRRIVEQdtMPPtgERQTLMFSATFPKEI-QMLAR 233
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
16-187 |
7.56e-44 |
|
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: 153.93 E-value: 7.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 16 LSNLNELGYTEMTPVQAAALP-AILNGQDVRAKAKTGSGKTAAFGIGLLDKI-------AVGEFVT--QALVLCPTRELA 85
Cdd:cd17946 2 LRALADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLlsqkssnGVGGKQKplRALILTPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 86 DQVSKELRRLARFTqNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGR----IQE---HLRKktlvLDDLKILVLDEADR 158
Cdd:cd17946 82 VQVKDHLKAIAKYT-NIKIASIVGGLAVQKQERLLKKRPEIVVATPGRlwelIQEgneHLAN----LKSLRFLVLDEADR 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 933675871 159 MLDMG-FT------DAIDDVIAYTPPQRQTLLFSAT 187
Cdd:cd17946 157 MLEKGhFAelekilELLNKDRAGKKRKRQTFVFSAT 192
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
16-206 |
2.84e-43 |
|
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: 150.98 E-value: 2.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 16 LSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQ-----ALVLCPTRELADQVSK 90
Cdd:cd17966 2 MDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINAQPPLERgdgpiVLVLAPTRELAQQIQQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 91 ELRRLARfTQNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMGFTDAIDD 170
Cdd:cd17966 82 EANKFGG-SSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 933675871 171 VIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNV 206
Cdd:cd17966 161 IVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
4-208 |
1.32e-42 |
|
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: 149.80 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 4 TSFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQALVLCPTRE 83
Cdd:cd17950 2 SGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 84 LADQVSKELRRLARFTQNIKILTLCGGQPMGHQLDSL-VHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRML-D 161
Cdd:cd17950 82 LAFQISNEYERFSKYMPNVKTAVFFGGVPIKKDIEVLkNKCPHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLeQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 933675871 162 MGFTDAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNVEV 208
Cdd:cd17950 162 LDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
6-206 |
3.27e-42 |
|
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: 148.36 E-value: 3.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 6 FSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQALVLCPTRELA 85
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 86 DQVSKELRRLARFTqNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMGFT 165
Cdd:cd18046 81 QQIQKVVMALGDYM-GIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 933675871 166 DAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNV 206
Cdd:cd18046 160 DQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
19-206 |
5.09e-42 |
|
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: 147.89 E-value: 5.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 19 LNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFV----TQALVLCPTRELADQ---VSKE 91
Cdd:cd17942 5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKprngTGVIIISPTRELALQiygVAKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 92 LRRLARFTQNIKIltlcGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLR-KKTLVLDDLKILVLDEADRMLDMGFTDAIDD 170
Cdd:cd17942 85 LLKYHSQTFGIVI----GGANRKAEAEKLGKGVNILVATPGRLLDHLQnTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 933675871 171 VIAYTPPQRQTLLFSATYPAGIEQIsARV--QRQPVNV 206
Cdd:cd17942 161 IIKLLPKRRQTMLFSATQTRKVEDL-ARIslKKKPLYV 197
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
17-206 |
5.41e-42 |
|
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: 148.12 E-value: 5.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 17 SNLNE-LGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIA---------VGEFvtqALVLCPTRELAD 86
Cdd:cd17949 3 SHLKSkMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLsleprvdrsDGTL---ALVLVPTRELAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 87 QVSKELRRLARFTQNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRK-KTLVLDDLKILVLDEADRMLDMGFT 165
Cdd:cd17949 80 QIYEVLEKLLKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNtQSFDVSNLRWLVLDEADRLLDMGFE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 933675871 166 DAIDDVIAY-------------TPPQRQTLLFSATYPAGIEQISARVQRQPVNV 206
Cdd:cd17949 160 KDITKILELlddkrskaggeksKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
11-206 |
7.46e-42 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called DEAD box RNA helicase DEAD5) and DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH)) are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350721 [Multi-domain] Cd Length: 196 Bit Score: 147.34 E-value: 7.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 11 LPAEQLSNLNELGYTEMTPVQAAALPAILNG--QDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQALVLCPTRELADQV 88
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTLKSPQALCLAPTRELARQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 89 SKELRRLARFTqNIKI-LTLCGGQ-PMGHQLDSlvhapHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDM-GFT 165
Cdd:cd17963 81 GEVVEKMGKFT-GVKVaLAVPGNDvPRGKKITA-----QIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGHG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 933675871 166 DAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNV 206
Cdd:cd17963 155 DQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
6-206 |
1.28e-41 |
|
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: 146.84 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 6 FSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQALVLCPTRELA 85
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 86 DQVSKELRRLARFTqNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMGFT 165
Cdd:cd18045 81 VQIQKVLLALGDYM-NVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 933675871 166 DAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNV 206
Cdd:cd18045 160 EQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
16-206 |
7.35e-41 |
|
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: 144.79 E-value: 7.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 16 LSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLdKIAVGE-----FVTQ----ALVLCPTRELAD 86
Cdd:cd17951 2 LKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLI-MFALEQekklpFIKGegpyGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 87 QVSKELRRLARFTQ-----NIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLD 161
Cdd:cd17951 81 QTHEVIEYYCKALQeggypQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 933675871 162 MGFTDAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNV 206
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
16-207 |
7.61e-40 |
|
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: 141.63 E-value: 7.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 16 LSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQALVLCPTRELADQVSKELRRL 95
Cdd:cd17943 2 LEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 96 ARFTQNIKILTLCGGQPMGHQLDSLvHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMGFTDAIDDVIAYT 175
Cdd:cd17943 82 GKKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSSL 160
|
170 180 190
....*....|....*....|....*....|..
gi 933675871 176 PPQRQTLLFSATYPAGIEQISARVQRQPVNVE 207
Cdd:cd17943 161 PKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
6-207 |
1.57e-39 |
|
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: 141.30 E-value: 1.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 6 FSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDkiavgefVTQALVLCPTRELA 85
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ-------IVVALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 86 DQVSKELRRLARFTQNIKI--LTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMG 163
Cdd:cd17938 74 EQTYNCIENFKKYLDNPKLrvALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 933675871 164 FTDAIDDVIAYTP-----PQR-QTLLFSAT-YPAGIEQISARVQRQPVNVE 207
Cdd:cd17938 154 NLETINRIYNRIPkitsdGKRlQVIVCSATlHSFEVKKLADKIMHFPTWVD 204
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
16-189 |
2.85e-37 |
|
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: 135.36 E-value: 2.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 16 LSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGE------FVTQALVLCPTRELADQVS 89
Cdd:cd17944 2 IKLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQqprkrgRAPKVLVLAPTRELANQVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 90 KELRRLarfTQNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMGFTDAID 169
Cdd:cd17944 82 KDFKDI---TRKLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVE 158
|
170 180
....*....|....*....|....*
gi 933675871 170 DVI--AY---TPPQRQTLLFSATYP 189
Cdd:cd17944 159 EILsvSYkkdSEDNPQTLLFSATCP 183
|
|
| RRM_EcDbpA_like |
cd12501 |
RNA recognition motif (RRM) found in Escherichia coli RNA helicase dbpA and similar proteins; ... |
387-459 |
1.87e-35 |
|
RNA recognition motif (RRM) found in Escherichia coli RNA helicase dbpA and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of dbpA. E. coli dbpA is a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. It binds with high affinity and specificity for RNA substrates containing hairpin 92 of 23S rRNA (HP92) with either 3' or 5' extensions. As a non-processive ATP-dependent helicase, DbpA destabilizes and unwinds short <9bp (base pairs) RNA duplexes as well as long duplex RNA stretches. It disrupts RNA helices exclusively in a 3'- 5' direction and requires a single-stranded loading site 3' of the substrate helix. dbpA contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain binds specifically to hairpin 92.
Pssm-ID: 409924 [Multi-domain] Cd Length: 73 Bit Score: 125.82 E-value: 1.87e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933675871 387 TLCIDGGRKAKIRPGDILGALTGEASLTAADVGKIDMFPVHAYVAIRKASAKRALQQLQQGKIKGKNCKARLL 459
Cdd:cd12501 1 TIQIDGGKKQKLRPGDILGALTGDNGIDGEDIGKINITDFVSYVAVKRSVAKDALKKLREGKIKGRKFRVRLL 73
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
6-208 |
1.04e-34 |
|
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: 129.36 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 6 FSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQA-----LVLCP 80
Cdd:cd18049 26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGdgpicLVLAP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 81 TRELADQVSKELRRLARFTQnIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRML 160
Cdd:cd18049 106 TRELAQQVQQVAAEYGRACR-LKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRML 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 933675871 161 DMGFTDAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNVEV 208
Cdd:cd18049 185 DMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
16-206 |
4.13e-33 |
|
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: 123.73 E-value: 4.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 16 LSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGI-GLLDKIA--------VGEFVtqaLVLCPTRELAD 86
Cdd:cd17958 2 MKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLpGFIHLDLqpipreqrNGPGV---LVLTPTRELAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 87 QVSKELRRLARftQNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMGFTD 166
Cdd:cd17958 79 QIEAECSKYSY--KGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 933675871 167 AIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNV 206
Cdd:cd17958 157 QIRKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
228-337 |
9.02e-33 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 120.01 E-value: 9.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 228 KRLPLLISVLSHYQPASCVVFCNTKKDCQSVYeALESRGISVLALHGDLEQRDRDQVLVRFANRSCRVLVATDVAARGLD 307
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 933675871 308 IKDLELVVNFELAFDPEVHVHRIGRTGRAG 337
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
4-208 |
2.42e-32 |
|
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: 123.97 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 4 TSFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQA-----LVL 78
Cdd:cd18050 62 FAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHINHQPYLERGdgpicLVL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 79 CPTRELADQVSKELRRLARfTQNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADR 158
Cdd:cd18050 142 APTRELAQQVQQVADDYGK-SSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADR 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 933675871 159 MLDMGFTDAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQPVNVEV 208
Cdd:cd18050 221 MLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
16-187 |
1.75e-30 |
|
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: 117.73 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 16 LSNLNELGYTEMTPVQAAALPAILNGQ---------DVRAKAKTGSGKTAAFGIGLLDKIAvGEFVTQ--ALVLCPTREL 84
Cdd:cd17956 2 LKNLQNNGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLPIVQALS-KRVVPRlrALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 85 ADQVSKELRRLARFTqNIKILTLCG---------GQPMGHQLDSLVhAPHIVVGTPGRIQEHLRKKT-LVLDDLKILVLD 154
Cdd:cd17956 81 VQQVYKVFESLCKGT-GLKVVSLSGqksfkkeqkLLLVDTSGRYLS-RVDILVATPGRLVDHLNSTPgFTLKHLRFLVID 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 933675871 155 EADRMLDMGFTDAIDDVIAYT------------------PPQR--QTLLFSAT 187
Cdd:cd17956 159 EADRLLNQSFQDWLETVMKALgrptapdlgsfgdanlleRSVRplQKLLFSAT 211
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
16-199 |
2.27e-30 |
|
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: 117.47 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 16 LSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKI-------AVGEFVTQALVLCPTRELADQV 88
Cdd:cd17948 2 VEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykllaEGPFNAPRGLVITPSRELAEQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 89 SKELRRLARFTqNIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRMLDMGFTDAI 168
Cdd:cd17948 82 GSVAQSLTEGL-GLKVKVITGGRTKRQIRNPHFEEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 933675871 169 DDVIAYTP-------------PQRQTLLFSATYPAGIEQISARV 199
Cdd:cd17948 161 SHFLRRFPlasrrsentdgldPGTQLVLVSATMPSGVGEVLSKV 204
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
2-203 |
2.54e-27 |
|
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350806 [Multi-domain] Cd Length: 229 Bit Score: 108.96 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 2 STTSFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNG--QDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQALVLC 79
Cdd:cd18048 16 SVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALKLYPQCLCLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 80 PTRELADQVSKELRRLARFTQNIKILTLCGGQ--PMGHQLDSlvhapHIVVGTPGRIQEHLRKKTLV-LDDLKILVLDEA 156
Cdd:cd18048 96 PTFELALQTGKVVEEMGKFCVGIQVIYAIRGNrpGKGTDIEA-----QIVIGTPGTVLDWCFKLRLIdVTNISVFVLDEA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 933675871 157 DRMLDM-GFTDAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQP 203
Cdd:cd18048 171 DVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
256-337 |
3.52e-26 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 101.13 E-value: 3.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 256 QSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRSCRVLVATDVAARGLDIKDLELVVNFELAFDPEVHVHRIGRTGR 335
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 933675871 336 AG 337
Cdd:smart00490 81 AG 82
|
|
| DbpA |
pfam03880 |
DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of ... |
387-458 |
1.29e-24 |
|
DbpA RNA binding domain; This RNA binding domain is found at the C-terminus of a number of DEAD helicase proteins. It is sufficient to confer specificity for hairpin 92 of 23S rRNA, which is part of the ribosomal A-site. However, several members of this family lack specificity for 23S rRNA. These can proteins can generally be distinguished by a basic region that extends beyond this domain [Karl Kossen, unpublished data].
Pssm-ID: 461082 [Multi-domain] Cd Length: 72 Bit Score: 96.29 E-value: 1.29e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933675871 387 TLCIDGGRKAKIRPGDILGALTGEASLTAADVGKIDMFPVHAYVAIRKASAKRALQQLQQGKIKGKNCKARL 458
Cdd:pfam03880 1 RLFINVGKKDGVRPGDIVGALANEAGLPGDDIGKIDIFDNFSFVEVPAEKAEKVLKALKGTKIKGRKVRVEP 72
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
5-203 |
8.02e-20 |
|
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: 87.47 E-value: 8.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 5 SFSSLTLPAEQLSNLNELGYTEMTPVQAAALPAILNG--QDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTQALVLCPTR 82
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 83 ELADQVSKELRRLARFTQNIKILTLCggqpMGHQLDSLVH-APHIVVGTPGRIQEHLRKKTLV-LDDLKILVLDEADRML 160
Cdd:cd18047 82 ELALQTGKVIEQMGKFYPELKLAYAV----RGNKLERGQKiSEQIVIGTPGTVLDWCSKLKFIdPKKIKVFVLDEADVMI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 933675871 161 -DMGFTDAIDDVIAYTPPQRQTLLFSATYPAGIEQISARVQRQP 203
Cdd:cd18047 158 aTQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
13-315 |
2.62e-19 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 90.47 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 13 AEQLSNLNELGYTEMT--PVQAAALPAIL-----NGQDVRAKAKTGSGKTAaFGIGLLDKIAVGEFVtqaLVLCPTRELA 85
Cdd:COG1061 65 AEALEAGDEASGTSFElrPYQQEALEALLaalerGGGRGLVVAPTGTGKTV-LALALAAELLRGKRV---LVLVPRRELL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 86 DQVSKELRRLARFTQNIkiltlcGGQpmgHQLDSlvhapHIVVGTPGRIQEHLRKKTLVlDDLKILVLDEADRmldmGFT 165
Cdd:COG1061 141 EQWAEELRRFLGDPLAG------GGK---KDSDA-----PITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 166 DAIDDVIAYTPPQRqTLLFSAT----------------------YPAGIEQ-ISARVQRQPVNVEVDD-GDEAPAIEQVF 221
Cdd:COG1061 202 PSYRRILEAFPAAY-RLGLTATpfrsdgreillflfdgivyeysLKEAIEDgYLAPPEYYGIRVDLTDeRAEYDALSERL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 222 FE--TTREKRLPLLISVL--SHYQPASCVVFCNTKKDCQSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRSCRVLV 297
Cdd:COG1061 281 REalAADAERKDKILRELlrEHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILV 360
|
330
....*....|....*...
gi 933675871 298 ATDVAARGLDIKDLELVV 315
Cdd:COG1061 361 TVDVLNEGVDVPRLDVAI 378
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
19-189 |
3.02e-17 |
|
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: 81.27 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 19 LNELGYTEMTPVQAAALPAIL---------------NGQDVRA-KAKTGSGKTAAFGIGLLDKI-----AVGEFVTQ--- 74
Cdd:cd17965 23 NKTDEEIKPSPIQTLAIKKLLktlmrkvtkqtsneePKLEVFLlAAETGSGKTLAYLAPLLDYLkrqeqEPFEEAEEeye 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 75 ---------ALVLCPTRELADQVSKELRRLARFTQ-NIKILTLCGGQPMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLV 144
Cdd:cd17965 103 sakdtgrprSVILVPTHELVEQVYSVLKKLSHTVKlGIKTFSSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPKI 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 933675871 145 LDDLKILVLDEADRMLDMGFTDAIDDVIAYTPPQRQTLLFSATYP 189
Cdd:cd17965 183 LSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIP 227
|
|
| RRM_DbpA |
cd12252 |
RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases; ... |
387-455 |
1.18e-16 |
|
RNA recognition motif (RRM) found in the DbpA subfamily of prokaryotic DEAD-box rRNA helicases; This subfamily corresponds to the C-terminal RRM homology domain of dbpA proteins implicated in ribosome biogenesis. They bind with high affinity and specificity to RNA substrates containing hairpin 92 of 23S rRNA (HP92), which is part of the ribosomal A-site. The majority of dbpA proteins contain two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding. Several members of this family lack specificity for 23S rRNA. These proteins can generally be distinguished by a basic region that extends beyond the C-terminal domain.
Pssm-ID: 409698 [Multi-domain] Cd Length: 71 Bit Score: 74.12 E-value: 1.18e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 933675871 387 TLCIDGGRKAKIRPGDILGALTGEASLTAADVGKIDMFPVHAYVAIRKASAKRALQQLQQGKIKGKNCK 455
Cdd:cd12252 1 RLFINVGRKDGIDPRDLLGAICRAGGISRDDIGAIRIFDNFSFVEVPEAEAERVIEALNGKKIKGKKLR 69
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
48-187 |
1.62e-16 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 76.29 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 48 AKTGSGKTAAFGIGLLDKIAVGEFvtQALVLCPTRELADQVSKELRRlaRFTQNIKILTLCGGQPMGHQLDSLVHAPHIV 127
Cdd:cd00046 8 APTGSGKTLAALLAALLLLLKKGK--KVLVLVPTKALALQTAERLRE--LFGPGIRVAVLVGGSSAEEREKNKLGDADII 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933675871 128 VGTPGRIQEHL-RKKTLVLDDLKILVLDEADRMLDMGFTDAIDD--VIAYTPPQRQTLLFSAT 187
Cdd:cd00046 84 IATPDMLLNLLlREDRLFLKDLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
19-366 |
3.57e-14 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 74.55 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 19 LNELGYTEMTPVQAAALPA-ILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEfvtQALVLCPTRELADQVSKELRR-LA 96
Cdd:COG1204 15 LKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKALLNGG---KALYIVPLRALASEKYREFKRdFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 97 RFTQNIKILTlcGGQPMGhqlDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEA------DRmldmGFTdaIDD 170
Cdd:COG1204 92 ELGIKVGVST--GDYDSD---DEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAhliddeSR----GPT--LEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 171 VIA---YTPPQRQTLLFSATYPaGIEQISA-------RVQRQPV--NVEV-DDGdeapaiEQVFFETTREKRLPLLISVL 237
Cdd:COG1204 161 LLArlrRLNPEAQIVALSATIG-NAEEIAEwldaelvKSDWRPVplNEGVlYDG------VLRFDDGSRRSKDPTLALAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 238 SHYQP-ASCVVFCNTKKDCQSV----------------YEALESRGISVLAL---------------------HGDLEQR 279
Cdd:COG1204 234 DLLEEgGQVLVFVSSRRDAESLakkladelkrrltpeeREELEELAEELLEVseethtnekladclekgvafhHAGLPSE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 280 DRDQVLVRFANRSCRVLVATD-------VAARGLDIKDLELVVNFELafdPEVHVHR-IGRTGRAGM--SGLAVSLCTPQ 349
Cdd:COG1204 314 LRRLVEDAFREGLIKVLVATPtlaagvnLPARRVIIRDTKRGGMVPI---PVLEFKQmAGRAGRPGYdpYGEAILVAKSS 390
|
410
....*....|....*..
gi 933675871 350 EMTRaHAIEDYLQMKLK 366
Cdd:COG1204 391 DEAD-ELFERYILGEPE 406
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
223-338 |
9.84e-14 |
|
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: 68.00 E-value: 9.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 223 ETTREKRLPLLISVLSHYQpASCVVFCNTKKDCQSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRSCRVLVATdVA 302
Cdd:cd18794 12 DKKDEKLDLLKRIKVEHLG-GSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT-VA 89
|
90 100 110
....*....|....*....|....*....|....*..
gi 933675871 303 -ARGLDIKDLELVVNFELAFDPEVHVHRIGRTGRAGM 338
Cdd:cd18794 90 fGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGL 126
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
223-349 |
3.89e-13 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 70.94 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 223 ETTREKRLPLLISVLSHYQPASCVVFCNTKKDCQSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRSCRVLVATdVA 302
Cdd:COG0514 211 PKPPDDKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IA 289
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 933675871 303 -ARGLDIKDLELVVNFELAFDPEVHVHRIGRTGRAGMSGLAVSLCTPQ 349
Cdd:COG0514 290 fGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPE 337
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
245-331 |
4.39e-11 |
|
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: 60.57 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 245 CVVFCNTKKDCQSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRS--CRVLVATDVAARGLDIKDLELVVNFELAFD 322
Cdd:cd18793 30 VLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPdiRVFLLSTKAGGVGLNLTAANRVILYDPWWN 109
|
90
....*....|....*
gi 933675871 323 PEVH------VHRIG 331
Cdd:cd18793 110 PAVEeqaidrAHRIG 124
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
26-156 |
1.96e-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: 59.58 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 26 EMTPVQAAALPAILNGQD-VRAKAKTGSGKTAAFGIGLLDKIAVGEFVtqALVLCPTRELADQVSKELR-RLARFTQNIK 103
Cdd:cd17921 1 LLNPIQREALRALYLSGDsVLVSAPTSSGKTLIAELAILRALATSGGK--AVYIAPTRALVNQKEADLReRFGPLGKNVG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 933675871 104 ILTlcGGQPMGHQLDSlvhAPHIVVGTPGRIQEHLRK-KTLVLDDLKILVLDEA 156
Cdd:cd17921 79 LLT--GDPSVNKLLLA---EADILVATPEKLDLLLRNgGERLIQDVRLVVVDEA 127
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
227-352 |
2.63e-09 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 59.34 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 227 EKRLPL--LISVLSHYQPASCVVFCNTKKDCQSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRSCRVLVATDVAAR 304
Cdd:PRK11057 219 EKFKPLdqLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGM 298
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 933675871 305 GLDIKDLELVVNFELAFDPEVHVHRIGRTGRAGMSGLAVSLCTPQEMT 352
Cdd:PRK11057 299 GINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMA 346
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
245-337 |
3.91e-09 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 58.97 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 245 CVVFCNTKKDCQSVYEALESRGISVLALHGD--------LEQRDRDQVLVRFANRSCRVLVATDVAARGLDIKDLELVVN 316
Cdd:COG1111 356 IIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIF 435
|
90 100
....*....|....*....|.
gi 933675871 317 FELAFDPEVHVHRIGRTGRAG 337
Cdd:COG1111 436 YEPVPSEIRSIQRKGRTGRKR 456
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
11-343 |
6.54e-08 |
|
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: 54.84 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 11 LPAEQLSNLNELGYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEFVTqALVLCPTRELA-DQVS 89
Cdd:COG1205 41 LPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDPGAT-ALYLYPTKALArDQLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 90 KeLRRLARFT-QNIKILTLCGGQPMgHQLDSLVHAPHIVVGTP-----GrIQEHLRKKTLVLDDLKILVLDEA------- 156
Cdd:COG1205 120 R-LRELAEALgLGVRVATYDGDTPP-EERRWIREHPDIVLTNPdmlhyG-LLPHHTRWARFFRNLRYVVIDEAhtyrgvf 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 157 --------DRMLdmgftdaidDVIAYTPPQRQTLLFSATypagI---EQISARVQRQPVNVEVDDGDEAPAIEQVFFE-- 223
Cdd:COG1205 197 gshvanvlRRLR---------RICRHYGSDPQFILASAT----IgnpAEHAERLTGRPVTVVDEDGSPRGERTFVLWNpp 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 224 ----TTREKRLPLLISVLSH--YQPASCVVFCNTKKDCQSVYEALESR------GISVLALHGDLEQRDRDQVLVRFANR 291
Cdd:COG1205 264 lvddGIRRSALAEAARLLADlvREGLRTLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERGLRSG 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 933675871 292 SCRVLVATDVAARGLDIKDLELVVnfelafdpevhVH-----------RIGRTGRAGMSGLAV 343
Cdd:COG1205 344 ELLGVVSTNALELGIDIGGLDAVV-----------LAgypgtrasfwqQAGRAGRRGQDSLVV 395
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
26-187 |
1.37e-07 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 51.13 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 26 EMTPVQAAALPAILNGQDVRAK-----AKTGSGKT--AAFGIGLLDKIAvgeFVTQALVLCPTRELADQVSKELRRLARF 98
Cdd:pfam04851 3 ELRPYQIEAIENLLESIKNGQKrglivMATGSGKTltAAKLIARLFKKG---PIKKVLFLVPRKDLLEQALEEFKKFLPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 99 TQNIKILTlcggqpMGHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVL--DEADRmldmGFTDAIDDVIAYTP 176
Cdd:pfam04851 80 YVEIGEII------SGDKKDESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIiiDEAHR----SGASSYRNILEYFK 149
|
170
....*....|.
gi 933675871 177 PQRQtLLFSAT 187
Cdd:pfam04851 150 PAFL-LGLTAT 159
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
31-156 |
1.49e-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: 51.43 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 31 QAAALPAILNGQDVRAKAKTGSGKTAAFGIGLLDKIAvGEFVTQALVLCPTRELA-DQVSKELRRLARFTQNIKILTLCG 109
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALL-RDPGSRALYLYPTKALAqDQLRSLRELLEQLGLGIRVATYDG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 933675871 110 GQPMGHQLDSLVHAPHIVVGTP-----GRIQEHLRKKTLvLDDLKILVLDEA 156
Cdd:cd17923 84 DTPREERRAIIRNPPRILLTNPdmlhyALLPHHDRWARF-LRNLRYVVLDEA 134
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
246-353 |
2.48e-07 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 53.34 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 246 VVFCNTKKDCQSVYEALESRGISVLALHGdleQRDRD-----------QVLVRFANRSCRVLVATDVAARGLDIKDLELV 314
Cdd:PRK13766 369 IVFTQYRDTAEKIVDLLEKEGIKAVRFVG---QASKDgdkgmsqkeqiEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLV 445
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 933675871 315 VNFElafdP---EVH-VHRIGRTGRaGMSGLAVSLCTpqEMTR 353
Cdd:PRK13766 446 IFYE----PvpsEIRsIQRKGRTGR-QEEGRVVVLIA--KGTR 481
|
|
| RRM_BsYxiN_like |
cd12500 |
RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and ... |
388-455 |
2.64e-07 |
|
RNA recognition motif (RRM) found in Bacillus subtilis ATP-dependent RNA helicase YxiN and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of YxiN. B. subtilis YxiN is a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. It binds with high affinity and specificity to RNA substrates containing hairpin 92 of 23S rRNA (HP92) with either 3' or 5' extensions in an ATP-dependent manner. YxiN contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding.
Pssm-ID: 409923 [Multi-domain] Cd Length: 73 Bit Score: 47.84 E-value: 2.64e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 933675871 388 LCIDGGRKAKIRPGDILGALTGEASLTAADVGKIDMFPVHAYVAIRKASAKRALQQLQQGKIKGKNCK 455
Cdd:cd12500 2 LYFNGGKKKKIRAVDIVGAISNIDGVTGDDIGIITVQDNCSYVDILNGKGDHVLKVMKNTTIKGKQVK 69
|
|
| RRM_EcCsdA_like |
cd12499 |
RNA recognition motif (RRM) found in Escherichia coli cold-shock DEAD box protein A (CsdA) and ... |
390-459 |
3.32e-07 |
|
RNA recognition motif (RRM) found in Escherichia coli cold-shock DEAD box protein A (CsdA) and similar proteins; This subgroup corresponds to the C-terminal RRM homology domain of E. coli CsdA, also termed ATP-dependent RNA helicase deaD, or translation factor W2, a member of the DbpA subfamily of prokaryotic DEAD-box rRNA helicases that have been implicated in ribosome biogenesis. CsdA may be involved in translation initiation, gene regulation after cold-shock, mRNA decay and biogenesis of the large or small ribosomal subunit. It contains two N-terminal ATPase catalytic domains and a C-terminal RNA binding domain, an atypical RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNPs (ribonucleoprotein domain). The catalytic domains bind to nearby regions of RNA to stimulate ATP hydrolysis and disrupt RNA structures. The C-terminal domain is responsible for the high-affinity RNA binding.
Pssm-ID: 409922 [Multi-domain] Cd Length: 73 Bit Score: 47.57 E-value: 3.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 390 IDGGRKAKIRPGDILGALTGEASLTAADVGKIDMFPVHAYVAIRKASAKRALQQLQQGKIKGKNCKARLL 459
Cdd:cd12499 4 IEVGRKDGVKPGNIVGAIANEAGIDSRFIGRIKIFDDHSTVELPKGMPKDVLQHLKKVRVCGQPLNIKLL 73
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
223-319 |
4.88e-07 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 49.13 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 223 ETTREKRLPLLISVLSHYQP----ASCVVFCNTKKDCQSVYEALES---------------RGISVLALHGDLEQRDRDQ 283
Cdd:cd18802 2 EIVVIPKLQKLIEILREYFPktpdFRGIIFVERRATAVVLSRLLKEhpstlafircgfligRGNSSQRKRSLMTQRKQKE 81
|
90 100 110
....*....|....*....|....*....|....*.
gi 933675871 284 VLVRFANRSCRVLVATDVAARGLDIKDLELVVNFEL 319
Cdd:cd18802 82 TLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDL 117
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
48-337 |
6.63e-07 |
|
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: 51.30 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 48 AKTGSGKTAAFGIGLLDKIAVGEFVTQALVLcPTRELADQVSKELRRL--------------ARFTQNIKILTLCGGQPM 113
Cdd:TIGR01587 6 APTGYGKTEAALLWALHSIKSQKADRVIIAL-PTRATINAMYRRAKELfgselvglhhsssfSRIKEMGDSEEFEHLFPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 114 -GHQLDSLVHAPhIVVGTPGRIQEHL------RKKTLVLDDLKILVLDEADRMLD--MGFTDAIDDVIAYTppQRQTLLF 184
Cdd:TIGR01587 85 yIHSNDKLFLDP-ITVCTIDQVLKSVfgefghYEFTLASIANSLLIFDEVHFYDEytLALILAVLEVLKDN--DVPILLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 185 SATYPAGIEQISARVQrQPVNVEVDDGDEAPAIEQVFFETTREKRLP---LLISVLSHY-QPASCVVFCNTKKDCQSVYE 260
Cdd:TIGR01587 162 SATLPKFLKEYAEKIG-YVEFNEPLDLKEERRFENHRFILIESDKVGeisSLERLLEFIkKGGSIAIIVNTVDRAQEFYQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 261 ALESRG--ISVLALHGDLEQRDRD----QVLVRFA-NRSCRVLVATDVAARGLDIkDLELVVNfELAfDPEVHVHRIGRT 333
Cdd:TIGR01587 241 QLKEKApeEEIILYHSRFTEKDRAkkeaELLREMKkSNEKFVIVATQVIEASLDI-SADVMIT-ELA-PIDSLIQRLGRL 317
|
....
gi 933675871 334 GRAG 337
Cdd:TIGR01587 318 HRYG 321
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
276-345 |
7.12e-07 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 48.51 E-value: 7.12e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 276 LEQRDRDQVLVRFANRSCRVLVATDVAARGLDIKDLELVVNFELAFDPEVHVHRIGRTGRaGMSGLAVSL 345
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVVVL 142
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
26-159 |
7.58e-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: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 26 EMTPVQAAALPAILngQDVRAK--------AKTGSGKTAAFGIGLLDKIAVGEfvtQALVLCPTRELADQVSKELRrlaR 97
Cdd:cd17918 15 SLTKDQAQAIKDIE--KDLHSPepmdrllsGDVGSGKTLVALGAALLAYKNGK---QVAILVPTEILAHQHYEEAR---K 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933675871 98 FTQNIKILTLCGGQPmghqlDSLVHAPHIVVGTPGRIQEHLRKKTLVLddlkiLVLDEADRM 159
Cdd:cd17918 87 FLPFINVELVTGGTK-----AQILSGISLLVGTHALLHLDVKFKNLDL-----VIVDEQHRF 138
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
48-337 |
1.15e-06 |
|
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: 50.51 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 48 AKTGSGKTAAFGIGLLDKIAVGEFVTQALVLcPTRELAD-------------QVSKELRRLARFTQNIKILTLCGGQPM- 113
Cdd:cd09639 6 APTGYGKTEAALLWALHSLKSQKADRVIIAL-PTRATINamyrrakeafgetGLYHSSILSSRIKEMGDSEEFEHLFPLy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 114 GHQLDSLVHAPhIVVGTPGRIQEHL------RKKTLVLDDLKILVLDEADRMLD--MGFTDAIDDVIAYTppQRQTLLFS 185
Cdd:cd09639 85 IHSNDTLFLDP-ITVCTIDQVLKSVfgefghYEFTLASIANSLLIFDEVHFYDEytLALILAVLEVLKDN--DVPILLMS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 186 ATYPAGIEQ----ISARVQRQPVNVEVDDGDEAPAIEQ--VFFETTREKRLPLLISvlshyqPASCVVFCNTKKDCQSVY 259
Cdd:cd09639 162 ATLPKFLKEyaekIGYVEENEPLDLKPNERAPFIKIESdkVGEISSLERLLEFIKK------GGSVAIIVNTVDRAQEFY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 260 EALESRG--ISVLALHGDLEQRDR----DQVLVRFANRSCRVLVATDVAARGLDIkDLELVVNfELAfDPEVHVHRIGRT 333
Cdd:cd09639 236 QQLKEKGpeEEIMLIHSRFTEKDRakkeAELLLEFKKSEKFVIVATQVIEASLDI-SVDVMIT-ELA-PIDSLIQRLGRL 312
|
....
gi 933675871 334 GRAG 337
Cdd:cd09639 313 HRYG 316
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
26-155 |
2.73e-06 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 47.71 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 26 EMTPVQAAALPA-ILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEfvtQALVLCPTRELADQVSKELRRLARFTQNIKI 104
Cdd:cd18028 1 ELYPPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLLEGG---KALYLVPLRALASEKYEEFKKLEEIGLKVGI 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 933675871 105 LTlcGGQPMGhqlDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDE 155
Cdd:cd18028 78 ST--GDYDED---DEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDE 123
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
245-333 |
3.84e-06 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 49.45 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 245 CVVFCNTKKDCQSVYEALESRGISVLALHGDLEQRDRDQVLVRFANRS--CRVLVATDVAARGLDIKDLELVVNFELAFD 322
Cdd:COG0553 552 VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGEGLNLTAADHVIHYDLWWN 631
|
90
....*....|....*..
gi 933675871 323 PEVH------VHRIGRT 333
Cdd:COG0553 632 PAVEeqaidrAHRIGQT 648
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
245-337 |
6.14e-06 |
|
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: 44.23 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 245 CVVFCNTKKDCQSVYEALEsrgisvlalhgdleqrdrdqvlvrfanrscrVLVATDVAARGLDIKDLELVVNFELAFDPE 324
Cdd:cd18785 6 IIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSAA 54
|
90
....*....|...
gi 933675871 325 VHVHRIGRTGRAG 337
Cdd:cd18785 55 SYIQRVGRAGRGG 67
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
211-347 |
2.00e-05 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 44.47 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 211 GDEAPAIEQVFFETTREKRLPLLISVLSHYQPasCVVFCNTKKDCQSVyeALESRGISVlaLHGDLEQRDRDQVLVRFAN 290
Cdd:cd18795 14 GLGIKLRVDVMNKFDSDIIVLLKIETVSEGKP--VLVFCSSRKECEKT--AKDLAGIAF--HHAGLTREDRELVEELFRE 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933675871 291 RSCRVLVATDVAARGLD-------IKDLELVVNFELAFDPEVHVHR-IGRTGRAGM--SGLAVSLCT 347
Cdd:cd18795 88 GLIKVLVATSTLAAGVNlpartviIKGTQRYDGKGYRELSPLEYLQmIGRAGRPGFdtRGEAIIMTK 154
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
239-315 |
2.04e-05 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 43.70 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 239 HYQPASCVVFCNTKKDCQSVYEALESRGISVLALHGDLEQRDR-DQVLVRFANR--SCRVLVATDVAARGLDIKDLELVV 315
Cdd:cd18799 3 KYVEIKTLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
7-187 |
2.90e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 46.49 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 7 SSLTLPAEQLSNLNELGYTEMTPVQAAALPA-ILNGQDVRAKAKTGSGKTAAFGIGLLDKIAVGEfvtQALVLCPTRELA 85
Cdd:PRK02362 4 AELPLPEGVIEFYEAEGIEELYPPQAEAVEAgLLDGKNLLAAIPTASGKTLIAELAMLKAIARGG---KALYIVPLRALA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 86 DQVSKELRRLARFTQNIKILTlcgGQPmgHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDE------ADR- 158
Cdd:PRK02362 81 SEKFEEFERFEELGVRVGIST---GDY--DSRDEWLGDNDIIVATSEKVDSLLRNGAPWLDDITCVVVDEvhlidsANRg 155
|
170 180 190
....*....|....*....|....*....|...
gi 933675871 159 -MLDMgftdaiddVIA---YTPPQRQTLLFSAT 187
Cdd:PRK02362 156 pTLEV--------TLAklrRLNPDLQVVALSAT 180
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
24-58 |
3.92e-04 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 42.78 E-value: 3.92e-04
10 20 30
....*....|....*....|....*....|....*.
gi 933675871 24 YTEMTPVQAAALPAILNGQDVRAKAKTGSGKT-AAF 58
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF 57
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
50-156 |
7.85e-04 |
|
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: 40.71 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 50 TGSGKT--AAFGI----GLLDKIAVGEfvTQALVLCPTRELADQVSKELRRlarFTqNIKILTLCG--GQPMGHQ--LDS 119
Cdd:cd18034 25 TGSGKTliAVMLIkemgELNRKEKNPK--KRAVFLVPTVPLVAQQAEAIRS---HT-DLKVGEYSGemGVDKWTKerWKE 98
|
90 100 110
....*....|....*....|....*....|....*..
gi 933675871 120 LVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEA 156
Cdd:cd18034 99 ELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
19-187 |
8.26e-04 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 41.73 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 19 LNELGYTEMTPVQAAALPA-ILNGQDVRAKAKTGSGKTAAFGIGLLDKIAvgEFVTQALVLCPTRELADQVSKELRRLAR 97
Cdd:PRK00254 16 LKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLL--REGGKAVYLVPLKALAEEKYREFKDWEK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 98 FtqNIKILTLCGGQpmgHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADRM--LDMGFTdaIDDVIAYT 175
Cdd:PRK00254 94 L--GLRVAMTTGDY---DSTDEWLGKYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIgsYDRGAT--LEMILTHM 166
|
170
....*....|..
gi 933675871 176 PPQRQTLLFSAT 187
Cdd:PRK00254 167 LGRAQILGLSAT 178
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
35-158 |
1.14e-03 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 39.81 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 35 LPAILNGQDVRAKAK---------TGSGKTAAFGIGLLDKIAvgEFVTQALVLCPTRELADQVSKELRRLarFTQNIKIL 105
Cdd:cd18035 1 EERRLYQVLIAAVALngntlivlpTGLGKTIIAILVAADRLT--KKGGKVLILAPSRPLVEQHAENLKRV--LNIPDKIT 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 933675871 106 TLCGG-QPmgHQLDSLVHAPHIVVGTPGRIQEHLRKKTLVLDDLKILVLDEADR 158
Cdd:cd18035 77 SLTGEvKP--EERAERWDASKIIVATPQVIENDLLAGRITLDDVSLLIFDEAHH 128
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
30-131 |
1.18e-03 |
|
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: 40.03 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 30 VQAAALPAILNGQD-VRAKAKTGSGKTAAFGIGLL----DKIAVGEFVTQALVLCPTRELADQVSKELRrlARFTQ-NIK 103
Cdd:cd18023 5 IQSEVFPDLLYSDKnFVVSAPTGSGKTVLFELAILrllkERNPLPWGNRKVVYIAPIKALCSEKYDDWK--EKFGPlGLS 82
|
90 100
....*....|....*....|....*...
gi 933675871 104 ILTLCGGQPMGhQLDSLVHApHIVVGTP 131
Cdd:cd18023 83 CAELTGDTEMD-DTFEIQDA-DIILTTP 108
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
243-335 |
1.20e-03 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 39.17 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 243 ASCVVFCNTKKDCQSVYEAL-ESRGISVLAL-----HGDLEQRDRDQVLVRFANRSCRVLVATDVAARGLDIKDLELVVN 316
Cdd:cd18796 39 KSTLVFTNTRSQAERLAQRLrELCPDRVPPDfialhHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQ 118
|
90
....*....|....*....
gi 933675871 317 FELAFDPEVHVHRIGRTGR 335
Cdd:cd18796 119 IGSPKSVARLLQRLGRSGH 137
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
253-352 |
1.29e-03 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 39.25 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 253 KDCQSVYEALESR---GISVLALHGDLEQRDRDQVLVRFANRSCRVLVATDVAARGLDIKDLELVV-----NFELAfdpE 324
Cdd:cd18811 45 KAAVAMYEYLKERfrpELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMViedaeRFGLS---Q 121
|
90 100
....*....|....*....|....*...
gi 933675871 325 VHVHRiGRTGRAGMSGLAVsLCTPQEMT 352
Cdd:cd18811 122 LHQLR-GRVGRGDHQSYCL-LVYKDPLT 147
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
253-358 |
1.29e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 39.56 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 253 KDCQSVYEALESR--GISVLALHGDLEQRDRDQVLVRFANRSCRVLVATDVAARGLDIKDLELVV-----NFELAfdpEV 325
Cdd:cd18792 45 KSIEALAEELKELvpEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIiedadRFGLS---QL 121
|
90 100 110
....*....|....*....|....*....|...
gi 933675871 326 HVHRiGRTGRAGMSGLAVSLCTPQEMTRAHAIE 358
Cdd:cd18792 122 HQLR-GRVGRGKHQSYCYLLYPDPKKLTETAKK 153
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
23-156 |
3.65e-03 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 38.67 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 23 GYTEMTPVQAAALPAILNGQDVRAKAKTGSGKTAAFGIG--LLDKIavgefvtqALVLCPTREL-ADQVSKeLRRLarft 99
Cdd:cd17920 9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV--------TLVVSPLISLmQDQVDR-LQQL---- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 933675871 100 qNIKILTLCGGQPMGHQLDSLV----HAPHIVVGTP-----GRIQEHLRKKTLvLDDLKILVLDEA 156
Cdd:cd17920 76 -GIRAAALNSTLSPEEKREVLLriknGQYKLLYVTPerllsPDFLELLQRLPE-RKRLALIVVDEA 139
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
24-155 |
3.88e-03 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 39.87 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 24 YTEMTPVQAAALPAILNGQDVRAKAKTGSGKT-AAF-GI-----------GLLDKIavgefvtQALVLCPTRELADQVSK 90
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFlAIidelfrlgregELEDKV-------YCLYVSPLRALNNDIHR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 91 -------ELRRLARftqnikiltlcggqPMGHQLDSLVHA------------------PHIVVGTPgriqEHL------- 138
Cdd:PRK13767 103 nleepltEIREIAK--------------ERGEELPEIRVAirtgdtssyekqkmlkkpPHILITTP----ESLaillnsp 164
|
170
....*....|....*....
gi 933675871 139 --RKKtlvLDDLKILVLDE 155
Cdd:PRK13767 165 kfREK---LRTVKWVIVDE 180
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
268-358 |
5.11e-03 |
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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: 37.32 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933675871 268 SVLALHGDLEQRDRDQVLVRFANRSCRVLVATDVAARGLDIKDLELVV-----NFELAfdpEVHVHRiGRTGRAGMSGLA 342
Cdd:cd18810 53 RIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIieradKFGLA---QLYQLR-GRVGRSKERAYA 128
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90
....*....|....*.
gi 933675871 343 VSLCTPQEMTRAHAIE 358
Cdd:cd18810 129 YFLYPDQKKLTEDALK 144
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