|
Name |
Accession |
Description |
Interval |
E-value |
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
30-233 |
1.55e-135 |
|
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: 401.30 E-value: 1.55e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVPQGGVRALILSPTRD 109
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVGARALILSPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 110 LAEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEvDDMTLRTVEYVVFDEADSLFGMG 189
Cdd:cd17959 83 LALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVE-MNLKLSSVEYVVFDEADRLFEMG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 334183955 190 FAEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLREPQLVR 233
Cdd:cd17959 162 FAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLIR 205
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
30-431 |
1.67e-135 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 409.54 E-value: 1.67e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVPqGGVRALILSPTRD 109
Cdd:COG0513 4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRP-RAPQALILAPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 110 LAEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEvDDMTLRTVEYVVFDEADSLFGMG 189
Cdd:COG0513 83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRMLDMG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 190 FAEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLREPQLVRLDVENKISPDLKLSFLTVRPEEKYSALLYLVREHis 269
Cdd:COG0513 162 FIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDE-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 270 SDQQTLIFVSTKHHVEFVNSLFKLENIEPSVCYGDMDQDARKIHVSRFRARKTMLLIVTDIAARGIDIPLLDNVINWDFP 349
Cdd:COG0513 240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 350 PRPKIFVHRVGRAARAGRTGCAYSFVTPEDMPYMLDLHLFLSK--PVRPAPTEDEVLKN-MEEVMTKTSQAIDSGVTVYG 426
Cdd:COG0513 320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQkiEEEELPGFEPVEEKrLERLKPKIKEKLKGKKAGRG 399
|
....*
gi 334183955 427 RFPQK 431
Cdd:COG0513 400 GRPGP 404
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
41-233 |
1.08e-83 |
|
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: 265.84 E-value: 1.08e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 41 NAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLK--QHVPQGGVRALILSPTRDLAEQTLKFT 118
Cdd:cd00268 3 KALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLpePKKKGRGPQALVLAPTRELAMQIAEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 119 KELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEvDDMTLRTVEYVVFDEADSLFGMGFAEQLHQIL 198
Cdd:cd00268 83 RKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIER-GKLDLSNVKYLVLDEADRMLDMGFEEDVEKIL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 334183955 199 TQLSENRQTLLFSATLPSALAEFAKAGLREPQLVR 233
Cdd:cd00268 162 SALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
30-398 |
6.13e-81 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 267.82 E-value: 6.13e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKqhVPQGGVRALILSPTRD 109
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLD--VKRFRVQALVLCPTRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 110 LAEQTLKFTKELGKFTD-LRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLM-HLlsEVDDMTLRTVEYVVFDEADSLFG 187
Cdd:PRK11776 84 LADQVAKEIRRLARFIPnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILdHL--RKGTLDLDALNTLVLDEADRMLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 188 MGFAEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLREPQLVRLDVENKiSPDLKLSFLTVRPEEKYSALLYLVREH 267
Cdd:PRK11776 162 MGFQDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHD-LPAIEQRFYEVSPDERLPALQRLLLHH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 268 isSDQQTLIFVSTKHHVEFVNSLFKLENIEPSVCYGDMDQDARKIHVSRFRARKTMLLIVTDIAARGIDIPLLDNVINWD 347
Cdd:PRK11776 241 --QPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYE 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 334183955 348 FPPRPKIFVHRVGRAARAGRTGCAYSFVTPEDMPYMLDLHLFLSKPVRPAP 398
Cdd:PRK11776 319 LARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKLNWEP 369
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
30-383 |
2.81e-76 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 254.48 E-value: 2.81e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLeklkQHV---PQ---GGVRALI 103
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPAL----QHLldfPRrksGPPRILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 104 LSPTRDLAEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEvDDMTLRTVEYVVFDEAD 183
Cdd:PRK11192 79 LTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKE-ENFDCRAVETLILDEAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 184 SLFGMGFAEQLHQILTQLSENRQTLLFSATLP-SALAEFAKAGLREPqlVRLDVE------NKIspdLKLSFLTVRPEEK 256
Cdd:PRK11192 158 RMLDMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDP--VEVEAEpsrrerKKI---HQWYYRADDLEHK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 257 YSALLYLVREhiSSDQQTLIFVSTKHHVEFVNSLFKLENIEPSVCYGDMDQDARKIHVSRFRARKTMLLIVTDIAARGID 336
Cdd:PRK11192 233 TALLCHLLKQ--PEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGID 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 334183955 337 IPLLDNVINWDFPPRPKIFVHRVGRAARAGRTGCAYSFVTPEDMPYM 383
Cdd:PRK11192 311 IDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLL 357
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
30-394 |
2.31e-74 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 250.11 E-value: 2.31e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVPQGG----VRALILS 105
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAKgrrpVRALILT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 106 PTRDLAEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEvDDMTLRTVEYVVFDEADSL 185
Cdd:PRK10590 83 PTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQ-NAVKLDQVEILVLDEADRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 186 FGMGFAEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLREPQLVRLDVENKISPDLKLSFLTVRPEEKYSALLYLVR 265
Cdd:PRK10590 162 LDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQMIG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 266 EhiSSDQQTLIFVSTKHHVEFVNSLFKLENIEPSVCYGDMDQDARKIHVSRFRARKTMLLIVTDIAARGIDIPLLDNVIN 345
Cdd:PRK10590 242 K--GNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 334183955 346 WDFPPRPKIFVHRVGRAARAGRTGCAYSFVTPEDMPYMLDLHLFLSKPV 394
Cdd:PRK10590 320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEI 368
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
30-405 |
2.27e-70 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 240.20 E-value: 2.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVPQ-----GGVRALIL 104
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPPPkerymGEPRALII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 105 SPTRDLAEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEEL-TKGPDVIIATPGRLMHLlSEVDDMTLRTVEYVVFDEAD 183
Cdd:PRK01297 169 APTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDF-NQRGEVHLDMVEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 184 SLFGMGFAEQLHQILTQL--SENRQTLLFSATLPSALAEFAKAGLREPQLVRLDVENKISPDLKLSFLTVRPEEKYSALL 261
Cdd:PRK01297 248 RMLDMGFIPQVRQIIRQTprKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAGSDKYKLLY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 262 YLVREhiSSDQQTLIFVSTKHHVEFVNSLFKLENIEPSVCYGDMDQDARKIHVSRFRARKTMLLIVTDIAARGIDIPLLD 341
Cdd:PRK01297 328 NLVTQ--NPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGIS 405
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334183955 342 NVINWDFPPRPKIFVHRVGRAARAGRTGCAYSFVTPEDMPYMLDLHLFLSKPVRPAPTEDEVLK 405
Cdd:PRK01297 406 HVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKISCEMPPAELLK 469
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
39-406 |
4.87e-68 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 235.82 E-value: 4.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 39 VFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIP-MLEKLKQHV--PQGGVRALILSPTRDLAEQTL 115
Cdd:PTZ00110 141 ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPaIVHINAQPLlrYGDGPIVLVLAPTRELAEQIR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 116 KFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLsEVDDMTLRTVEYVVFDEADSLFGMGFAEQLH 195
Cdd:PTZ00110 221 EQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFL-ESNVTNLRRVTYLVLDEADRMLDMGFEPQIR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 196 QILTQLSENRQTLLFSATLPSALAEFAKAGLREpQLVRLDVEN---KISPDLKLSFLTVRPEEKYSALLYLVREHISSDQ 272
Cdd:PTZ00110 300 KIVSQIRPDRQTLMWSATWPKEVQSLARDLCKE-EPVHVNVGSldlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMRDGD 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 273 QTLIFVSTKHHVEFVNSLFKLENIePSVC-YGDMDQDARKIHVSRFRARKTMLLIVTDIAARGIDIPLLDNVINWDFPPR 351
Cdd:PTZ00110 379 KILIFVETKKGADFLTKELRLDGW-PALCiHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQ 457
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 334183955 352 PKIFVHRVGRAARAGRTGCAYSFVTPEDMPYMLDLHLFLSKPVRPAPTEDEVLKN 406
Cdd:PTZ00110 458 IEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPELEKLSN 512
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
30-404 |
4.37e-65 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 228.30 E-value: 4.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKL---------KQHVPqggvR 100
Cdd:PRK04537 11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpaladrKPEDP----R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 101 ALILSPTRDLAEQ----TLKFTKELGkftdLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEVDDMTLRTVEY 176
Cdd:PRK04537 87 ALILAPTRELAIQihkdAVKFGADLG----LRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 177 VVFDEADSLFGMGFAEQLHQILTQLSE--NRQTLLFSATLPSALAEFAKAGLREPQLVRLDVENKISPDLKLSFLTVRPE 254
Cdd:PRK04537 163 CVLDEADRMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 255 EKYSALLYLVREhiSSDQQTLIFVSTKHHVEFVNSLFKLENIEPSVCYGDMDQDARKIHVSRFRARKTMLLIVTDIAARG 334
Cdd:PRK04537 243 EKQTLLLGLLSR--SEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 335 IDIPLLDNVINWDFPPRPKIFVHRVGRAARAGRTGCAYSFVTPEDMPYMLDLHLFLSKPVRPAPTEDEVL 404
Cdd:PRK04537 321 LHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPVTAELL 390
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
42-235 |
4.29e-64 |
|
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: 213.27 E-value: 4.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 42 AIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVPQGGV-RALILSPTRDLAEQTLKFTKE 120
Cdd:cd17947 4 ALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAAtRVLVLVPTRELAMQCFSVLQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 121 LGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEVDDMTLRTVEYVVFDEADSLFGMGFAEQLHQILTQ 200
Cdd:cd17947 84 LAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEILRL 163
|
170 180 190
....*....|....*....|....*....|....*
gi 334183955 201 LSENRQTLLFSATLPSALAEFAKAGLREPqlVRLD 235
Cdd:cd17947 164 CPRTRQTMLFSATMTDEVKDLAKLSLNKP--VRVF 196
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
30-375 |
1.01e-63 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 225.88 E-value: 1.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHV--PQggvrALILSPT 107
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLDPELkaPQ----ILVLAPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 108 RDLAEQTLKFTKELGK-FTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLM-HLLSEVDDmtLRTVEYVVFDEADSL 185
Cdd:PRK11634 84 RELAVQVAEAMTDFSKhMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLdHLKRGTLD--LSKLSGLVLDEADEM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 186 FGMGFAEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLREPQLVRLDVENKISPDLKLSFLTVRPEEKYSALL-YLV 264
Cdd:PRK11634 162 LRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVrFLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 265 REHISSdqqTLIFVSTKHHVEFVNSLFKLENIEPSVCYGDMDQDARKIHVSRFRARKTMLLIVTDIAARGIDIPLLDNVI 344
Cdd:PRK11634 242 AEDFDA---AIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVV 318
|
330 340 350
....*....|....*....|....*....|.
gi 334183955 345 NWDFPPRPKIFVHRVGRAARAGRTGCAYSFV 375
Cdd:PRK11634 319 NYDIPMDSESYVHRIGRTGRAGRAGRALLFV 349
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
52-221 |
6.15e-63 |
|
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: 209.02 E-value: 6.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 52 TPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQhvPQGGVRALILSPTRDLAEQTLKFTKELGKFTDLRVSL 131
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDK--LDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 132 LVGGDSMEDQFEELtKGPDVIIATPGRLMHLLSEVDdmTLRTVEYVVFDEADSLFGMGFAEQLHQILTQLSENRQTLLFS 211
Cdd:pfam00270 79 LLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLQERK--LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLS 155
|
170
....*....|
gi 334183955 212 ATLPSALAEF 221
Cdd:pfam00270 156 ATLPRNLEDL 165
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
30-400 |
6.83e-63 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 217.39 E-value: 6.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVpqGGVRALILSPTRD 109
Cdd:PTZ00424 30 FDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDL--NACQALILAPTRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 110 LAEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSE----VDDMTLrtveyVVFDEADSL 185
Cdd:PTZ00424 108 LAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKrhlrVDDLKL-----FILDEADEM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 186 FGMGFAEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLREPQLVRLDVENKISPDLKLSFLTVRPEEKYSALLYLVR 265
Cdd:PTZ00424 183 LSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 266 EHISSdQQTLIFVSTKHHVEFVNSLFKLENIEPSVCYGDMDQDARKIHVSRFRARKTMLLIVTDIAARGIDIPLLDNVIN 345
Cdd:PTZ00424 263 ETLTI-TQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVIN 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 334183955 346 WDFPPRPKIFVHRVGRAARAGRTGCAYSFVTPEDMPYMLDLHLFLSKPVRPAPTE 400
Cdd:PTZ00424 342 YDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQIEEMPME 396
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
43-236 |
7.06e-63 |
|
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: 210.14 E-value: 7.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 43 IKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVPQGGVRALILSPTRDLAEQTLKFTKELG 122
Cdd:cd17957 5 LEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKKGLRALILAPTRELASQIYRELLKLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 123 KFTDLRVSLLVGGDS-MEDQFEELTKGPDVIIATPGRLMHLLSEvDDMTLRTVEYVVFDEADSLFGMGFAEQLHQILTQL 201
Cdd:cd17957 85 KGTGLRIVLLSKSLEaKAKDGPKSITKYDILVSTPLRLVFLLKQ-GPIDLSSVEYLVLDEADKLFEPGFREQTDEILAAC 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 334183955 202 SE-NRQTLLFSATLPSALAEFAKAGLREPqlVRLDV 236
Cdd:cd17957 164 TNpNLQRSLFSATIPSEVEELARSVMKDP--IRIIV 197
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
41-229 |
1.48e-59 |
|
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: 201.27 E-value: 1.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 41 NAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKL---KQHVPQGGVRALILSPTRDLAEQTLKF 117
Cdd:cd17960 3 DVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrKANLKKGQVGALIISPTRELATQIYEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 118 TKELGKFTD--LRVSLLVGGDSMEDQFEELT-KGPDVIIATPGRLMHLLS-EVDDMTLRTVEYVVFDEADSLFGMGFAEQ 193
Cdd:cd17960 83 LQSFLEHHLpkLKCQLLIGGTNVEEDVKKFKrNGPNILVGTPGRLEELLSrKADKVKVKSLEVLVLDEADRLLDLGFEAD 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 334183955 194 LHQILTQLSENRQTLLFSATLPSALAEFAKAGLREP 229
Cdd:cd17960 163 LNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNP 198
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
30-229 |
1.60e-59 |
|
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: 201.01 E-value: 1.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVPqgGVRALILSPTRD 109
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQ--RFFALVLAPTRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 110 LAEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEVDDMTLRTVEYVVFDEADSLFGMG 189
Cdd:cd17954 80 LAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLNMD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 334183955 190 FAEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLREP 229
Cdd:cd17954 160 FEPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNP 199
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
39-229 |
1.28e-57 |
|
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: 196.44 E-value: 1.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 39 VFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVPQG---GVRALILSPTRDLAEQTL 115
Cdd:cd17953 23 VLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRPVKpgeGPIGLIMAPTRELALQIY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 116 KFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEVDD--MTLRTVEYVVFDEADSLFGMGFAEQ 193
Cdd:cd17953 103 VECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILTANNGrvTNLRRVTYVVLDEADRMFDMGFEPQ 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 334183955 194 LHQILTQLSENRQTLLFSATLPSALAEFAKAGLREP 229
Cdd:cd17953 183 IMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKP 218
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
30-387 |
3.69e-57 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 202.12 E-value: 3.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQH-VPQG----GVRALIL 104
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHpAPEDrkvnQPRALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 105 SPTRDLAEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEvDDMTLRTVEYVVFDEADS 184
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQ-NHINLGAIQVVVLDEADR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 185 LFGMGFAEQLHQILTQLSE--NRQTLLFSATLPSALAEFAKAGLREPQLVRLDVENKISPDLKLSFLTVRPEEKYSALLY 262
Cdd:PRK04837 169 MFDLGFIKDIRWLFRRMPPanQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPSNEEKMRLLQT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 263 LVREHISsdQQTLIFVSTKHHVEFVNSLFKLENIEPSVCYGDMDQDARKIHVSRFRARKTMLLIVTDIAARGIDIPLLDN 342
Cdd:PRK04837 249 LIEEEWP--DRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTH 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 334183955 343 VINWDFPPRPKIFVHRVGRAARAGRTGCAYSFVTPEdmpYMLDLH 387
Cdd:PRK04837 327 VFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEE---YALNLP 368
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
30-231 |
3.89e-57 |
|
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: 194.37 E-value: 3.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHvPQgGVRALILSPTRD 109
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSED-PY-GIFALVLTPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 110 LAEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEVDDMT--LRTVEYVVFDEADSLFG 187
Cdd:cd17955 79 LAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDTTkvLSRVKFLVLDEADRLLT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 334183955 188 MGFAEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLREPQL 231
Cdd:cd17955 159 GSFEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFF 202
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
39-229 |
1.24e-56 |
|
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: 193.69 E-value: 1.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 39 VFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVP------QGGVRALILSPTRDLAE 112
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPldeetkDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 113 QTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLM-----HLLSevddmtLRTVEYVVFDEADSLFG 187
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLdclerRLLV------LNQCTYVVLDEADRMID 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334183955 188 MGFAEQLHQILTQL--------------------SENRQTLLFSATLPSALAEFAKAGLREP 229
Cdd:cd17945 155 MGFEPQVTKILDAMpvsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLRRP 216
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
35-228 |
9.91e-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: 188.18 E-value: 9.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 35 LGPNVFNAIKKKGYKVPTPIQRKTMPLILS-GVDVVAMARTGSGKTAAFLIPMLEKL---KQHVPQGGVRALILSPTRDL 110
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLlntKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 111 AEQTLK-FTKELGKFTDLRVSLLVGGDSMEDQFEELTK-GPDVIIATPGRLM-HLLSEVDDMTLRTVEYVVFDEADSLFG 187
Cdd:cd17964 81 ALQIAAeAKKLLQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIdHLENPGVAKAFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 334183955 188 MGFAEQLHQILTQL----SENRQTLLFSATLPSALAEFAKAGLRE 228
Cdd:cd17964 161 MGFRPDLEQILRHLpeknADPRQTLLFSATVPDEVQQIARLTLKK 205
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
41-229 |
1.46e-54 |
|
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: 187.24 E-value: 1.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 41 NAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKL---KQHVPQGGVRALILSPTRDLAEQTLKF 117
Cdd:cd17952 3 NAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImdqRELEKGEGPIAVIVAPTRELAQQIYLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 118 TKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLsEVDDMTLRTVEYVVFDEADSLFGMGFAEQLHQI 197
Cdd:cd17952 83 AKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMV-KKKATNLQRVTYLVLDEADRMFDMGFEYQVRSI 161
|
170 180 190
....*....|....*....|....*....|..
gi 334183955 198 LTQLSENRQTLLFSATLPSALAEFAKAGLREP 229
Cdd:cd17952 162 VGHVRPDRQTLLFSATFKKKIEQLARDILSDP 193
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
42-232 |
1.82e-53 |
|
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: 184.03 E-value: 1.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 42 AIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKL--KQHVPQGGVRALILSPTRDLAEQTLKFTK 119
Cdd:cd17941 4 GLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLyrERWTPEDGLGALIISPTRELAMQIFEVLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 120 ELGKFTDLRVSLLVGGDSMEDQFEELTkGPDVIIATPGRLMHLLSEVDDMTLRTVEYVVFDEADSLFGMGFAEQLHQILT 199
Cdd:cd17941 84 KVGKYHSFSAGLIIGGKDVKEEKERIN-RMNILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDAIVE 162
|
170 180 190
....*....|....*....|....*....|...
gi 334183955 200 QLSENRQTLLFSATLPSALAEFAKAGLREPQLV 232
Cdd:cd17941 163 NLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
30-227 |
1.95e-53 |
|
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: 185.00 E-value: 1.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKL--KQHVPQGGVR------A 101
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLleDGPPSVGRGRrkaypsA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 102 LILSPTRDLAEQ----TLKFTKElgkfTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLsEVDDMTLRTVEYV 177
Cdd:cd17967 82 LILAPTRELAIQiyeeARKFSYR----SGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFI-ERGRISLSSIKFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 334183955 178 VFDEADSLFGMGFAEQLHQILTQLS----ENRQTLLFSATLPSALAEFAKAGLR 227
Cdd:cd17967 157 VLDEADRMLDMGFEPQIRKIVEHPDmppkGERQTLMFSATFPREIQRLAADFLK 210
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
42-234 |
3.14e-52 |
|
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: 180.86 E-value: 3.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 42 AIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQH----VPQGGVRALILSPTRDLAEQTLKF 117
Cdd:cd17961 8 AIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAkaesGEEQGTRALILVPTRELAQQVSKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 118 TKELGKFT--DLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEVDDMTLRTVEYVVFDEADSLFGMGFAEQLH 195
Cdd:cd17961 88 LEQLTAYCrkDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLSYGYEEDLK 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 334183955 196 QILTQLSENRQTLLFSATLPSALAEFAKAGLREPQLVRL 234
Cdd:cd17961 168 SLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPAILKL 206
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
30-379 |
5.56e-51 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 187.30 E-value: 5.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVPQG-----GVRALIL 104
Cdd:PLN00206 123 FSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSGHpseqrNPLAMVL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 105 SPTRDLAEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEvDDMTLRTVEYVVFDEADS 184
Cdd:PLN00206 203 TPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSK-HDIELDNVSVLVLDEVDC 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 185 LFGMGFAEQLHQILTQLSENrQTLLFSATLPSALAEFAKAGLREPQLVRLDVENKISPDLKLSFLTVRPEEKYSALLYLV 264
Cdd:PLN00206 282 MLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDIL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 265 REHISSDQQTLIFVSTKHHVEFV-NSLFKLENIEPSVCYGDMDQDARKIHVSRFRARKTMLLIVTDIAARGIDIPLLDNV 343
Cdd:PLN00206 361 KSKQHFKPPAVVFVSSRLGADLLaNAITVVTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQV 440
|
330 340 350
....*....|....*....|....*....|....*.
gi 334183955 344 INWDFPPRPKIFVHRVGRAARAGRTGCAYSFVTPED 379
Cdd:PLN00206 441 IIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEED 476
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
43-245 |
7.20e-51 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 177.30 E-value: 7.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 43 IKKKGYKVPTPIQRKTMPLILSGV-DVVAMARTGSGKTAAFLIPMLEKLKQHvpqGGVRALILSPTRDLAEQTLKFTKEL 121
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGLrDVILAAPTGSGKTLAALLPALEALKRG---KGGRVLVLVPTRELAEQWAEELKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 122 GKFTDLRVSLLVGGDSMEDQFEELTKG-PDVIIATPGRLMHLLSEvDDMTLRTVEYVVFDEADSLFGMGFAEQLHQILTQ 200
Cdd:smart00487 78 GPSLGLKVVGLYGGDSKREQLRKLESGkTDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 334183955 201 LSENRQTLLFSATLPSALAEFAKAGLREPqlVRLDVENKISPDLK 245
Cdd:smart00487 157 LPKNVQLLLLSATPPEEIENLLELFLNDP--VFIDVGFTPLEPIE 199
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
30-230 |
1.49e-50 |
|
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: 176.33 E-value: 1.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVPqgGVRALILSPTRD 109
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKD--VIQALILVPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 110 LAEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSE-VDDmtLRTVEYVVFDEADSLFGM 188
Cdd:cd17940 79 LALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKgVAD--LSHCKTLVLDEADKLLSQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 334183955 189 GFAEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLREPQ 230
Cdd:cd17940 157 DFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPY 198
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
39-232 |
5.33e-49 |
|
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: 172.14 E-value: 5.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 39 VFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPML------EKLKQHVPQGGVRALILSPTRDLAE 112
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLImfaleqEKKLPFIKGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 113 QTLK----FTKEL--GKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEvDDMTLRTVEYVVFDEADSLF 186
Cdd:cd17951 81 QTHEvieyYCKALqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNK-KKINLDICRYLCLDEADRMI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 334183955 187 GMGFAEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLREPQLV 232
Cdd:cd17951 160 DMGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
39-229 |
3.42e-48 |
|
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: 169.47 E-value: 3.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 39 VFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLK--QHVPQG-GVRALILSPTRDLAEQTL 115
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINaqPPLERGdGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 116 KFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLsEVDDMTLRTVEYVVFDEADSLFGMGFAEQLH 195
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFL-DQGKTNLRRVTYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|....
gi 334183955 196 QILTQLSENRQTLLFSATLPSALAEFAKAGLREP 229
Cdd:cd17966 160 KIVDQIRPDRQTLMWSATWPKEVRRLAEDFLKDY 193
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
39-230 |
1.80e-47 |
|
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: 168.96 E-value: 1.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 39 VFNAIKKKGYKVPTPIQRKTMPLILS-GVDVVAMARTGSGKTAAFLIPMLEKLKQHV-------PQGGVRALILSPTRDL 110
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAAIRdGKDVIGAAETGSGKTLAFGIPILERLLSQKssngvggKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 111 AEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEVDDMT--LRTVEYVVFDEADSLFGM 188
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLanLKSLRFLVLDEADRMLEK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 334183955 189 GFAEQLHQILTQLSEN-------RQTLLFSATLpsALAEFAKAGLREPQ 230
Cdd:cd17946 161 GHFAELEKILELLNKDragkkrkRQTFVFSATL--TLDHQLPLKLNSKK 207
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
43-232 |
4.99e-47 |
|
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: 166.18 E-value: 4.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 43 IKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVPQGGvrALILSPTRDLAEQTLKFTKELG 122
Cdd:cd17962 5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPS--ALILTPTRELAVQIEDQAKELM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 123 K-FTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEvDDMTLRTVEYVVFDEADSLFGMGFAEQLHQILTQL 201
Cdd:cd17962 83 KgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQ-SSVELDNIKIVVVDEADTMLKMGFQQQVLDILENI 161
|
170 180 190
....*....|....*....|....*....|.
gi 334183955 202 SENRQTLLFSATLPSALAEFAKAGLREPQLV 232
Cdd:cd17962 162 SHDHQTILVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
30-228 |
6.13e-45 |
|
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: 162.83 E-value: 6.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQH-----------VPQgg 98
Cdd:cd18052 45 FEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgltassfsevqEPQ-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 99 vrALILSPTRDLAEQTLkftKELGKF---TDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEvDDMTLRTVE 175
Cdd:cd18052 123 --ALIVAPTRELANQIF---LEARKFsygTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGR-GKISLSKLK 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 334183955 176 YVVFDEADSLFGMGFAEQLHQILTQLS----ENRQTLLFSATLPSALAEFAKAGLRE 228
Cdd:cd18052 197 YLILDEADRMLDMGFGPEIRKLVSEPGmpskEDRQTLMFSATFPEEIQRLAAEFLKE 253
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
42-231 |
1.42e-44 |
|
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350700 [Multi-domain] Cd Length: 198 Bit Score: 159.45 E-value: 1.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 42 AIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLE---KLKqHVPQGGVRALILSPTRDLAEQTLKFT 118
Cdd:cd17942 4 AIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIEllyKLK-FKPRNGTGVIIISPTRELALQIYGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 119 KELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEVDDMTLRTVEYVVFDEADSLFGMGFAEQLHQIL 198
Cdd:cd17942 83 KELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQII 162
|
170 180 190
....*....|....*....|....*....|...
gi 334183955 199 TQLSENRQTLLFSATLPSALAEFAKAGLREPQL 231
Cdd:cd17942 163 KLLPKRRQTMLFSATQTRKVEDLARISLKKKPL 195
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
244-375 |
1.55e-44 |
|
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: 156.51 E-value: 1.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 244 LKLSFLTVRPEEKYSALLYLVREHISsDQQTLIFVSTKHHVEFVNSLFKLENIEPSVCYGDMDQDARKIHVSRFRARKTM 323
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLK-PGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 334183955 324 LLIVTDIAARGIDIPLLDNVINWDFPPRPKIFVHRVGRAARAGRTGCAYSFV 375
Cdd:cd18787 80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
33-229 |
2.28e-44 |
|
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: 158.64 E-value: 2.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 33 LNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKL--KQHVPQggvrALILSPTRDL 110
Cdd:cd17939 2 MGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdtTVRETQ----ALVLAPTREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 111 AEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEvDDMTLRTVEYVVFDEADSLFGMGF 190
Cdd:cd17939 78 AQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQR-RSLRTDKIKMFVLDEADEMLSRGF 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 334183955 191 AEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLREP 229
Cdd:cd17939 157 KDQIYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDP 195
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
39-232 |
4.11e-44 |
|
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: 158.01 E-value: 4.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 39 VFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIP-MLEKLKQHVP---QGGVRALILSPTRDLAEQT 114
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgFIHLDLQPIPreqRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 115 LKFTKELgKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHlLSEVDDMTLRTVEYVVFDEADSLFGMGFAEQL 194
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGFEPQI 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 334183955 195 HQILTQLSENRQTLLFSATLPSALAEFAKAGLREPQLV 232
Cdd:cd17958 159 RKILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
30-216 |
5.49e-44 |
|
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: 157.87 E-value: 5.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKlkqhvpqggVRALILSPTRD 109
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI---------VVALILEPSRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 110 LAEQTLKFTKELGKFTD---LRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEvDDMTLRTVEYVVFDEADSLF 186
Cdd:cd17938 72 LAEQTYNCIENFKKYLDnpkLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKT-GKLDLSSVRFFVLDEADRLL 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 334183955 187 GMGFAEQLHQILTQL-----SENR-QTLLFSATLPS 216
Cdd:cd17938 151 SQGNLETINRIYNRIpkitsDGKRlQVIVCSATLHS 186
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
39-233 |
1.29e-43 |
|
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, Component Of Gems 3, Gemin-3, and SMN-Interacting Protein) interacts directly with SMN (survival of motor neurons), the spinal muscular atrophy gene product, and may play a catalytic role in the function of the SMN complex on ribonucleoproteins. Diseases associated with DDX20 include spinal muscular atrophy and muscular atrophy. DDX20 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350701 [Multi-domain] Cd Length: 192 Bit Score: 156.27 E-value: 1.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 39 VFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHvpQGGVRALILSPTRDLAEQTLKFT 118
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLE--RRHPQVLILAPTREIAVQIHDVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 119 KELG-KFTDLRVSLLVGGDSMEDQFEELtKGPDVIIATPGRLMHLLsEVDDMTLRTVEYVVFDEADSLFGMGFAEQLHQI 197
Cdd:cd17943 79 KKIGkKLEGLKCEVFIGGTPVKEDKKKL-KGCHIAVGTPGRIKQLI-ELGALNVSHVRLFVLDEADKLMEGSFQKDVNWI 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 334183955 198 LTQLSENRQTLLFSATLPSALAEFAKAGLREPQLVR 233
Cdd:cd17943 157 FSSLPKNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
30-223 |
1.14e-42 |
|
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: 155.58 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPML---------EKLKQHVPQGGVR 100
Cdd:cd18051 23 FSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILsqiyeqgpgESLPSESGYYGRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 101 -----ALILSPTRDLAEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLsEVDDMTLRTVE 175
Cdd:cd18051 103 kqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDML-ERGKIGLDYCK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 334183955 176 YVVFDEADSLFGMGFAEQLHQILTQL----SENRQTLLFSATLPSALAEFAK 223
Cdd:cd18051 182 YLVLDEADRMLDMGFEPQIRRIVEQDtmppTGERQTLMFSATFPKEIQMLAR 233
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
30-228 |
1.81e-42 |
|
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: 154.78 E-value: 1.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLkQHVP----QGGVRALILS 105
Cdd:cd18049 26 FYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHI-NHQPflerGDGPICLVLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 106 PTRDLAEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLsEVDDMTLRTVEYVVFDEADSL 185
Cdd:cd18049 105 PTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFL-EAGKTNLRRCTYLVLDEADRM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 334183955 186 FGMGFAEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLRE 228
Cdd:cd18049 184 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
30-228 |
1.27e-39 |
|
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: 147.85 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLkQHVPQ----GGVRALILS 105
Cdd:cd18050 64 FHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHI-NHQPYlergDGPICLVLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 106 PTRDLAEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLsEVDDMTLRTVEYVVFDEADSL 185
Cdd:cd18050 143 PTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFL-EAGKTNLRRCTYLVLDEADRM 221
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 334183955 186 FGMGFAEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLRE 228
Cdd:cd18050 222 LDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRD 264
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
30-229 |
1.13e-38 |
|
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: 142.58 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVPQggVRALILSPTRD 109
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKA--TQALVLAPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 110 LAEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLsevDDMTLRT--VEYVVFDEADSLFG 187
Cdd:cd18046 79 LAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMI---NRRYLRTdyIKMFVLDEADEMLS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 334183955 188 MGFAEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLREP 229
Cdd:cd18046 156 RGFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDP 197
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
44-233 |
3.78e-37 |
|
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: 138.87 E-value: 3.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 44 KKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVPQ----GGVRALILSPTRDLAEQTLK-FT 118
Cdd:cd17949 7 SKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRvdrsDGTLALVLVPTRELALQIYEvLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 119 KELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEVDDMTLRTVEYVVFDEADSLFGMGFAEQLHQIL 198
Cdd:cd17949 87 KLLKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 334183955 199 -------------TQLSENRQTLLFSATLPSALAEFAKAGLREPQLVR 233
Cdd:cd17949 167 ellddkrskaggeKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
43-227 |
1.85e-35 |
|
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: 133.43 E-value: 1.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 43 IKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLK---QHVPQG-GVRALILSPTRDLAEQTLKFT 118
Cdd:cd17944 5 LQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQedqQPRKRGrAPKVLVLAPTRELANQVTKDF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 119 KELGKftDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEvDDMTLRTVEYVVFDEADSLFGMGFAEQLHQIL 198
Cdd:cd17944 85 KDITR--KLSVACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQN-GRLDLTKLKHVVLDEVDQMLDMGFAEQVEEIL 161
|
170 180 190
....*....|....*....|....*....|....
gi 334183955 199 TQL-----SENRQTLLFSATLPSALAEFAKAGLR 227
Cdd:cd17944 162 SVSykkdsEDNPQTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
35-223 |
7.00e-35 |
|
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: 131.54 E-value: 7.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 35 LGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVD--VVAMARTGSGKTAAFLIPMLEK--LKQHVPQggvrALILSPTRDL 110
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDPPenLIAQSQSGTGKTAAFVLAMLSRvdPTLKSPQ----ALCLAPTREL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 111 AEQTLKFTKELGKFTDLRVSLLVggDSMEDQFEELTKGPdVIIATPGRLMHLLSE--VDdmtLRTVEYVVFDEADSLFGM 188
Cdd:cd17963 77 ARQIGEVVEKMGKFTGVKVALAV--PGNDVPRGKKITAQ-IVIGTPGTVLDWLKKrqLD---LKKIKILVLDEADVMLDT 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 334183955 189 -GFAEQLHQILTQLSENRQTLLFSATLPSALAEFAK 223
Cdd:cd17963 151 qGHGDQSIRIKRMLPRNCQILLFSATFPDSVRKFAE 186
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
41-232 |
1.14e-34 |
|
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: 132.37 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 41 NAIKKKGYKVPTPIQRKTMPLILSGV---------DVVAMARTGSGKTAAFLIPMLEKLKQH-VPQggVRALILSPTRDL 110
Cdd:cd17956 3 KNLQNNGITSAFPVQAAVIPWLLPSSkstppyrpgDLCVSAPTGSGKTLAYVLPIVQALSKRvVPR--LRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 111 AEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKG--------PDVIIATPGRLMHLLSEVDDMTLRTVEYVVFDEA 182
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDtsgrylsrVDILVATPGRLVDHLNSTPGFTLKHLRFLVIDEA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334183955 183 DSLFGMGFAEQLHQI--------------------LTQLSENRQTLLFSATL---PSALAEFakaGLREPQLV 232
Cdd:cd17956 161 DRLLNQSFQDWLETVmkalgrptapdlgsfgdanlLERSVRPLQKLLFSATLtrdPEKLSSL---KLHRPRLF 230
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
30-229 |
4.69e-34 |
|
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: 129.51 E-value: 4.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVPQggVRALILSPTRD 109
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRE--TQALILSPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 110 LAEQTLKFTKELGKFTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLLSEvDDMTLRTVEYVVFDEADSLFGMG 189
Cdd:cd18045 79 LAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADEMLNKG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 334183955 190 FAEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLREP 229
Cdd:cd18045 158 FKEQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDP 197
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
42-220 |
4.24e-33 |
|
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350706 [Multi-domain] Cd Length: 231 Bit Score: 127.87 E-value: 4.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 42 AIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKL--KQHVPQGGV---RALILSPTRDLAEQTLK 116
Cdd:cd17948 4 ILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrYKLLAEGPFnapRGLVITPSRELAEQIGS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 117 FTKELGKFTDLRVSLLVGGDSMED----QFEEltkgPDVIIATPGRLMHLLSEvDDMTLRTVEYVVFDEADSLFGMGFAE 192
Cdd:cd17948 84 VAQSLTEGLGLKVKVITGGRTKRQirnpHFEE----VDILVATPGALSKLLTS-RIYSLEQLRHLVLDEADTLLDDSFNE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 334183955 193 QLHQIL--TQLSENR-----------QTLLFSATLPSALAE 220
Cdd:cd17948 159 KLSHFLrrFPLASRRsentdgldpgtQLVLVSATMPSGVGE 199
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
30-229 |
1.93e-27 |
|
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: 110.51 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKqHVPqGGVRALILSPTRD 109
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLE-PVD-GQVSVLVICHTRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 110 LAEQTLKFTKELGKF-TDLRVSLLVGGDSMEDQFEEL-TKGPDVIIATPGRLMHLLSEvDDMTLRTVEYVVFDEADSLFG 187
Cdd:cd17950 82 LAFQISNEYERFSKYmPNVKTAVFFGGVPIKKDIEVLkNKCPHIVVGTPGRILALVRE-KKLKLSHVKHFVLDECDKMLE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 334183955 188 -MGFAEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLREP 229
Cdd:cd17950 161 qLDMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDP 203
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
255-366 |
1.10e-26 |
|
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: 104.99 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 255 EKYSALLYLVREHisSDQQTLIFVSTKHHVEFvNSLFKLENIEPSVCYGDMDQDARKIHVSRFRARKTMLLIVTDIAARG 334
Cdd:pfam00271 1 EKLEALLELLKKE--RGGKVLIFSQTKKTLEA-ELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
|
90 100 110
....*....|....*....|....*....|..
gi 334183955 335 IDIPLLDNVINWDFPPRPKIFVHRVGRAARAG 366
Cdd:pfam00271 78 LDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
30-238 |
1.84e-25 |
|
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: 106.31 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKK---KGYK------VPTPIQRKTMPLILSG-----------------VDVVAmARTGSGKTAAFL 83
Cdd:cd17965 1 FDQLKLLPSVREAIIKeilKGSNktdeeiKPSPIQTLAIKKLLKTlmrkvtkqtsneepkleVFLLA-AETGSGKTLAYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 84 IPMLEKLKQ---------------HVPQGGVRALILSPTRDLAEQTLKFTKELGKFTDLRVSLLVG--GDSMEDQFEELT 146
Cdd:cd17965 80 APLLDYLKRqeqepfeeaeeeyesAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSgfGPSYQRLQLAFK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 147 KGPDVIIATPGRLMHLlSEVDDMTLRTVEYVVFDEADSLFGMGFAEQLHQILTQLSENRQTLLFSATLPSalaEFAKAgL 226
Cdd:cd17965 160 GRIDILVTTPGKLASL-AKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPK---EFDKT-L 234
|
250
....*....|....
gi 334183955 227 RE--PQLVRLDVEN 238
Cdd:cd17965 235 RKlfPDVVRIATPR 248
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
34-405 |
1.82e-24 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 109.54 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 34 NLGPNVFNAIKKKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHvpqGGVRALILSPTRDLA-E 112
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLED---PGATALYLYPTKALArD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 113 QtlkftkeLGKFTDLRVSLLVG-------GDSMEDQFEELTKGPDVIIATPgrlmhllsevdDM--------------TL 171
Cdd:COG1205 117 Q-------LRRLRELAEALGLGvrvatydGDTPPEERRWIREHPDIVLTNP-----------DMlhygllphhtrwarFF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 172 RTVEYVVFDEA---DSLFGMGFA---EQLHQILTQLSENRQTLLFSATLPSAlAEFAKA--GlREPQLVRLDVenkiSPD 243
Cdd:COG1205 179 RNLRYVVIDEAhtyRGVFGSHVAnvlRRLRRICRHYGSDPQFILASATIGNP-AEHAERltG-RPVTVVDEDG----SPR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 244 LKLSFLTVRPEEKY-----SALL---YLVREHISSDQQTLIFVSTKHHVEFVNSLFKLENIEPSVC-----Y--GDMDQD 308
Cdd:COG1205 253 GERTFVLWNPPLVDdgirrSALAeaaRLLADLVREGLRTLVFTRSRRGAELLARYARRALREPDLAdrvaaYraGYLPEE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 309 ARKIHvSRFRARKtmLLIVtdiAAR-----GIDIPLLDNVINWDFPPRPKIFVHRVGRAARAGRTGCAYsFVTPEDmP-- 381
Cdd:COG1205 333 RREIE-RGLRSGE--LLGV---VSTnalelGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVV-LVAGDD-Pld 404
|
410 420
....*....|....*....|....*....
gi 334183955 382 --YMLDLHLFLSKPVRPA---PTEDEVLK 405
Cdd:COG1205 405 qyYVRHPEELFERPPEAAvidPDNPYVLA 433
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
30-237 |
2.65e-24 |
|
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: 102.41 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSG--VDVVAMARTGSGKTAAFLIPMLEKL--KQHVPQggvrALILS 105
Cdd:cd18048 20 FEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVdaLKLYPQ----CLCLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 106 PTRDLAEQTLKFTKELGKF-TDLRVSLLVGGDsmedqfeELTKGPD----VIIATPGRLMHLLSEVDDMTLRTVEYVVFD 180
Cdd:cd18048 96 PTFELALQTGKVVEEMGKFcVGIQVIYAIRGN-------RPGKGTDieaqIVIGTPGTVLDWCFKLRLIDVTNISVFVLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 334183955 181 EADSLFGM-GFAEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLREPQLVRLDVE 237
Cdd:cd18048 169 EADVMINVqGHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDPNIIKLKKE 226
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
30-233 |
2.24e-21 |
|
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: 93.25 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 30 FESLNLGPNVFNAIKKKGYKVPTPIQRKTMPLILSG--VDVVAMARTGSGKTAAFLIPMLEKLKQHVPQGgvRALILSPT 107
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYP--QCLCLSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 108 RDLAEQTLKFTKELGKF-TDLRVSLLVGGDSMEdqfEELTKGPDVIIATPGRLMHLLSEVDDMTLRTVEYVVFDEADSLF 186
Cdd:cd18047 81 YELALQTGKVIEQMGKFyPELKLAYAVRGNKLE---RGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 334183955 187 G-MGFAEQLHQILTQLSENRQTLLFSATLPSALAEFAKAGLREPQLVR 233
Cdd:cd18047 158 AtQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIK 205
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
68-485 |
5.64e-21 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 97.79 E-value: 5.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 68 VVAMArTGSGKT--AAFLIpmlEKLKQhvpqgGVRALILSPTRDLAEQTLKftkELGKFTDLRvslLVGGDSMEDQFeel 145
Cdd:COG1061 104 LVVAP-TGTGKTvlALALA---AELLR-----GKRVLVLVPRRELLEQWAE---ELRRFLGDP---LAGGGKKDSDA--- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 146 tkgpDVIIATPGRLMHLLSevDDMTLRTVEYVVFDEADSLFgmgfAEQLHQILTQLSENRqTLLFSAT------LPSALA 219
Cdd:COG1061 166 ----PITVATYQSLARRAH--LDELGDRFGLVIIDEAHHAG----APSYRRILEAFPAAY-RLGLTATpfrsdgREILLF 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 220 EF------------AKAG-LREPQLVRLDVE--------NKISPDLKlSFLTVRPEEKYSALLYLVREHiSSDQQTLIFV 278
Cdd:COG1061 235 LFdgivyeyslkeaIEDGyLAPPEYYGIRVDltderaeyDALSERLR-EALAADAERKDKILRELLREH-PDDRKTLVFC 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 279 STKHHVEFVNSLFKLENIEPSVCYGDMDQDARKIHVSRFRARKTMLLIVTDIAARGIDIPLLDNVINWdfppRPK----I 354
Cdd:COG1061 313 SSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILL----RPTgsprE 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 355 FVHRVGRAARA---GRTGCAYSFVTpEDMPYMLDLHLFLSKPVRPAPTEDEVLKNMEEVMTKTSQAIDSGVTVYGRFPQK 431
Cdd:COG1061 389 FIQRLGRGLRPapgKEDALVYDFVG-NDVPVLEELAKDLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLE 467
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 334183955 432 TIDLIFNRTREMIDSSAELDSLERTSTKAFRLYSKTKPSPSKESIRRAKDLPRE 485
Cdd:COG1061 468 ELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALA 521
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
285-366 |
4.06e-19 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 82.26 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 285 EFVNSLFKLENIEPSVCYGDMDQDARKIHVSRFRARKTMLLIVTDIAARGIDIPLLDNVINWDFPPRPKIFVHRVGRAAR 364
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 334183955 365 AG 366
Cdd:smart00490 81 AG 82
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
67-213 |
1.67e-18 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 82.84 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 67 DVVAMARTGSGKTAAFLIPMLeklkQHVPQGGVRALILSPTRDLAEQTLKFTKELGKfTDLRVSLLVGGDSMEDQFEELT 146
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAAL----LLLLKKGKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334183955 147 KGPDVIIATPGRLMHLLSEVDDMTLRTVEYVVFDEADSLFGMGFAEQLH--QILTQLSENRQTLLFSAT 213
Cdd:cd00046 78 GDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILdlAVRKAGLKNAQVILLSAT 146
|
|
| DBP10CT |
pfam08147 |
DBP10CT (NUC160) domain; This C terminal domain is found in the Dbp10p subfamily of ... |
638-700 |
6.63e-17 |
|
DBP10CT (NUC160) domain; This C terminal domain is found in the Dbp10p subfamily of hypothetical RNA helicases.
Pssm-ID: 462373 [Multi-domain] Cd Length: 66 Bit Score: 75.40 E-value: 6.63e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334183955 638 DLVADDGQGIKQQQSNYH---WDKKGKKYIKLNNGDRvTASGKIKTESGAKATAK-KTGIYKRWQER 700
Cdd:pfam08147 1 DLTGDDGQELNQQKQVQKkmrWDKKKKKFVKRSGNDE-DGKKKIRTESGVKIPASyKSGRYDEWKKK 66
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
55-223 |
1.70e-16 |
|
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: 78.40 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 55 QRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVpqgGVRALILSPTRDLA-EQTLKFTKELGKF-TDLRVSLL 132
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDP---GSRALYLYPTKALAqDQLRSLRELLEQLgLGIRVATY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 133 VGGDSMEDQFEELTKGPDVIIATPGRLMHLL---SEVDDMTLRTVEYVVFDEA---DSLFGMGFA---EQLHQILTQLSE 203
Cdd:cd17923 82 DGDTPREERRAIIRNPPRILLTNPDMLHYALlphHDRWARFLRNLRYVVLDEAhtyRGVFGSHVAlllRRLRRLCRRYGA 161
|
170 180
....*....|....*....|
gi 334183955 204 NRQTLLFSATLpSALAEFAK 223
Cdd:cd17923 162 DPQFILTSATI-GNPAEHAR 180
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
35-285 |
2.17e-16 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 83.02 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 35 LGPNVFNAIKKKGYKVPTPIQRKTMP-LILSGVDVVAMARTGSGKTAAFLIPMLeklkQHVPQGGvRALILSPTRDLA-E 112
Cdd:COG1204 7 PLEKVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAIL----KALLNGG-KALYIVPLRALAsE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 113 QTLKFTKELGKFtDLRVSLLVGGDSMEDqfEELTKgPDVIIATPGRLMHLLSEVDDMtLRTVEYVVFDEAdslfgmgfae 192
Cdd:COG1204 82 KYREFKRDFEEL-GIKVGVSTGDYDSDD--EWLGR-YDILVATPEKLDSLLRNGPSW-LRDVDLVVVDEA---------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 193 qlHQI------------LTQLSE---NRQTLLFSATLPSA--LAEFAKAGLrepqlvrldVENKISP-DLKLSFLTVR-- 252
Cdd:COG1204 147 --HLIddesrgptlevlLARLRRlnpEAQIVALSATIGNAeeIAEWLDAEL---------VKSDWRPvPLNEGVLYDGvl 215
|
250 260 270
....*....|....*....|....*....|....*...
gi 334183955 253 -----PEEKYSALLYLVREHISSDQQTLIFVSTKHHVE 285
Cdd:COG1204 216 rfddgSRRSKDPTLALALDLLEEGGQVLVFVSSRRDAE 253
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
52-223 |
5.54e-14 |
|
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: 70.75 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 52 TPIQRKTM-PLILSGVDVVAMARTGSGKTAAFLIPMLEKLKQHvpqgGVRALILSPTRDLAEQTLKFTKELGKFTDLRVS 130
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATS----GGKAVYIAPTRALVNQKEADLRERFGPLGKNVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 131 LLVGGDSMEDQFEEltkGPDVIIATPGRLMHLLSEVDDMTLRTVEYVVFDEADSLF----GMgFAEQLHQILTQLSENRQ 206
Cdd:cd17921 79 LLTGDPSVNKLLLA---EADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAHLIGdgerGV-VLELLLSRLLRINKNAR 154
|
170
....*....|....*....
gi 334183955 207 TLLFSATLPSA--LAEFAK 223
Cdd:cd17921 155 FVGLSATLPNAedLAEWLG 173
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
48-362 |
5.22e-12 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 69.75 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 48 YKVPTPIQRKTMPLILSGVDVVAMARTGSGKT-AAFLIPMLEKLKQHVPQG---GVRALILSPTRDLA-------EQTLk 116
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPALDELARRPRPGElpdGLRVLYISPLKALAndiernlRAPL- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 117 ftKELGKFTDLRVSLL-VG---GDSmeDQFE---ELTKGPDVIIATPGRLMHLLSEVD-DMTLRTVEYVVFDEadslfgm 188
Cdd:COG1201 101 --EEIGEAAGLPLPEIrVGvrtGDT--PASErqrQRRRPPHILITTPESLALLLTSPDaRELLRGVRTVIVDE------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 189 gfaeqLHQIL-----TQLS---ENRQTLL--------FSATL--PSALAEFAkAGLREPQLVRLdVENKISPDLKLSflT 250
Cdd:COG1201 170 -----IHALAgskrgVHLAlslERLRALAprplqrigLSATVgpLEEVARFL-VGYEDPRPVTI-VDAGAGKKPDLE--V 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 251 VRPEEK---------------YSALLYLVREHISsdqqTLIFVSTKHHVEFVnsLFKL-----ENIEPSVCY-GDMDQDA 309
Cdd:COG1201 241 LVPVEDlierfpwaghlwphlYPRVLDLIEAHRT----TLVFTNTRSQAERL--FQRLnelnpEDALPIAAHhGSLSREQ 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334183955 310 R-----KIHVSRFRArktmllIVT----DIaarGIDIPLLDNVINWDFPPRPKIFVHRVGRA 362
Cdd:COG1201 315 RleveeALKAGELRA------VVAtsslEL---GIDIGDVDLVIQVGSPKSVARLLQRIGRA 367
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
65-221 |
1.50e-10 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 60.67 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 65 GVDVVAMARTGSGKTAAFLIPMLEKLKQHvPQGGVRALILSPTRDLAEQTLKFTKEL--GKFTDLRVSLLVGGDSMEDQF 142
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADE-PEKGVQVLYISPLKALINDQERRLEEPldEIDLEIPVAVRHGDTSQSEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 143 EELTKGPDVIIATPGRLMHLL-SEVDDMTLRTVEYVVFDE----ADSLFGMGFAEQLHQILTQLSENRQTLLFSATL--P 215
Cdd:cd17922 80 KQLKNPPGILITTPESLELLLvNKKLRELFAGLRYVVVDEihalLGSKRGVQLELLLERLRKLTGRPLRRIGLSATLgnL 159
|
....*.
gi 334183955 216 SALAEF 221
Cdd:cd17922 160 EEAAAF 165
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
68-214 |
4.32e-10 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 58.86 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 68 VVAMArTGSGKTAaFLIPMLEKLKQHvpqggvRALILSPTRDLAEQTLkftKELGKFTDLRVSLLVGGDSMEDQfeeltK 147
Cdd:cd17926 22 ILVLP-TGSGKTL-TALALIAYLKEL------RTLIVVPTDALLDQWK---ERFEDFLGDSSIGLIGGGKKKDF-----D 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334183955 148 GPDVIIATPGRLMHLLSEVDDMTLRTvEYVVFDEADSLFGMGFAEqlhqILTQLSENRQtLLFSATL 214
Cdd:cd17926 86 DANVVVATYQSLSNLAEEEKDLFDQF-GLLIVDEAHHLPAKTFSE----ILKELNAKYR-LGLTATP 146
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
54-179 |
1.05e-09 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 58.91 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 54 IQRKTMPLIL-SGVDVVAMARTGSGKTAAFLIPMLEKLKQH--VPQGGVRALILSPTRDLAEQTLKFTKElgKFTDLRVS 130
Cdd:cd18023 5 IQSEVFPDLLySDKNFVVSAPTGSGKTVLFELAILRLLKERnpLPWGNRKVVYIAPIKALCSEKYDDWKE--KFGPLGLS 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 334183955 131 LL-VGGDSMEDQFEELtKGPDVIIATPGRLmhllsevDDMTLRTVEYVVF 179
Cdd:cd18023 83 CAeLTGDTEMDDTFEI-QDADIILTTPEKW-------DSMTRRWRDNGNL 124
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
45-362 |
2.64e-09 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 61.06 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 45 KKGYKVPTPIQRKTMPLILSGVDVVAMARTGSGKT-AAFL--IPMLEKLKQHvpqGG----VRALILSPTRDLA------ 111
Cdd:PRK13767 27 KEKFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLaiIDELFRLGRE---GEledkVYCLYVSPLRALNndihrn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 112 -EQTLKFTKELGK-----FTDLRVSLLVGGDSMEDQFEELTKGPDVIIATPGRLMHLL-----SEvddmTLRTVEYVVFD 180
Cdd:PRK13767 104 lEEPLTEIREIAKergeeLPEIRVAIRTGDTSSYEKQKMLKKPPHILITTPESLAILLnspkfRE----KLRTVKWVIVD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 181 EADSLFG-------MGFAEQLhQILTQLSENRQTLlfSATLpSALAEFAK--AGLREPQLVRlDVE-------NKIspDL 244
Cdd:PRK13767 180 EIHSLAEnkrgvhlSLSLERL-EELAGGEFVRIGL--SATI-EPLEEVAKflVGYEDDGEPR-DCEivdarfvKPF--DI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 245 KL----SFLTVRPEEK-----YSALLYLVREHissdQQTLIFVSTKHHVEFVnsLFKL-------ENIEPSVC-YGDMDQ 307
Cdd:PRK13767 253 KVispvDDLIHTPAEEisealYETLHELIKEH----RTTLIFTNTRSGAERV--LYNLrkrfpeeYDEDNIGAhHSSLSR 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 334183955 308 DARkIHVSRFRARKTMLLIVTDIAAR-GIDIPLLDNVINWDFPPRPKIFVHRVGRA 362
Cdd:PRK13767 327 EVR-LEVEEKLKRGELKVVVSSTSLElGIDIGYIDLVVLLGSPKSVSRLLQRIGRA 381
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
72-341 |
4.46e-09 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 59.50 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 72 ARTGSGKTAaflipMLEKLKQHVPQGGVRALILSPTRDLAeqtlkftKELGK-----FTDLRVSLLVGGDsmedqfEELT 146
Cdd:COG4098 136 AVCGAGKTE-----MLFPAIAEALKQGGRVCIATPRVDVV-------LELAPrlqqaFPGVDIAALYGGS------EEKY 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 147 KGPDVIIATpgrlMHLLsevddmtLR---TVEYVVFDEADSlFGMGFAEQLHQILTQ-LSENRQTLLFSATLPSALAEFA 222
Cdd:COG4098 198 RYAQLVIAT----THQL-------LRfyqAFDLLIIDEVDA-FPYSGDPMLQYAVKRaRKPDGKLIYLTATPSKALQRQV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 223 KAGlrEPQLVRLDV----------ENKISPDLKLSFLTVRPEEKysaLLYLVREHISSDQQTLIFVSTKHHVEFVNSLFK 292
Cdd:COG4098 266 KRG--KLKVVKLPAryhghplpvpKFKWLGNWKKRLRRGKLPRK---LLKWLKKRLKEGRQLLIFVPTIELLEQLVALLQ 340
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 334183955 293 L----ENIEpSVCYGDMDqdaRKIHVSRFRARKTMLLIVTDIAARGIDIPLLD 341
Cdd:COG4098 341 KlfpeERIA-GVHAEDPE---RKEKVQAFRDGEIPILVTTTILERGVTFPNVD 389
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
74-182 |
8.18e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 56.04 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 74 TGSGKTAAFLIPMLEKLKQHvpqGGvRALILSPTRDLAEQTLKFTKELGKFTDLRVSLLVGGDSMEDQfEELTKGPDVII 153
Cdd:PRK13766 38 TGLGKTAIALLVIAERLHKK---GG-KVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTGEVSPEKR-AELWEKAKVIV 112
|
90 100 110
....*....|....*....|....*....|....*...
gi 334183955 154 ATP---------GRLmhllsevddmTLRTVEYVVFDEA 182
Cdd:PRK13766 113 ATPqviendliaGRI----------SLEDVSLLIFDEA 140
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
51-219 |
1.12e-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: 52.42 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 51 PTPIQRKTMPLILSGV------DVVAMARTGSGKTAAFLIPMLEKLKQhvpqgGVRALILSPTRDLAEQTLKFTKELgkF 124
Cdd:cd17918 16 LTKDQAQAIKDIEKDLhspepmDRLLSGDVGSGKTLVALGAALLAYKN-----GKQVAILVPTEILAHQHYEEARKF--L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 125 TDLRVSLLVGGDSmedqfEELTKGPDVIIATPGrLMHLLSEVDDMTLrtveyVVFDEADSlFGMGFAEQLHQIltqlsEN 204
Cdd:cd17918 89 PFINVELVTGGTK-----AQILSGISLLVGTHA-LLHLDVKFKNLDL-----VIVDEQHR-FGVAQREALYNL-----GA 151
|
170
....*....|....*.
gi 334183955 205 RQTLLFSAT-LPSALA 219
Cdd:cd17918 152 THFLEATATpIPRTLA 167
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
67-182 |
2.87e-07 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 51.88 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 67 DVVAMARTGSGKT--AAFLIPMLEKLKQHVPQGGVRALILSPTRDLAEQTlkfTKELGKFTDLRVSLLVGGDSMEDQ--- 141
Cdd:cd18034 18 NTIVVLPTGSGKTliAVMLIKEMGELNRKEKNPKKRAVFLVPTVPLVAQQ---AEAIRSHTDLKVGEYSGEMGVDKWtke 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 334183955 142 -FEELTKGPDVIIATPGRLMHLLS----EVDDMTLrtveyVVFDEA 182
Cdd:cd18034 95 rWKEELEKYDVLVMTAQILLDALRhgflSLSDINL-----LIFDEC 135
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
74-182 |
2.98e-07 |
|
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: 51.36 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 74 TGSGKTAAFLIPMLEKLKQHvpqgGVRALILSPTRDLAEQTLKFTKELGKFTDLRVSLLvgGDSMEDQFEELTKGPDVII 153
Cdd:cd18035 25 TGLGKTIIAILVAADRLTKK----GGKVLILAPSRPLVEQHAENLKRVLNIPDKITSLT--GEVKPEERAERWDASKIIV 98
|
90 100 110
....*....|....*....|....*....|
gi 334183955 154 ATPGRLMH-LLSEvdDMTLRTVEYVVFDEA 182
Cdd:cd18035 99 ATPQVIENdLLAG--RITLDDVSLLIFDEA 126
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
253-366 |
4.59e-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: 49.90 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 253 PEEKYSALLYLVREH--ISSDQQTLIFVSTKHHVEFVNSLFKLENIE---------------PSVCYGDMDQDARKIHVS 315
Cdd:cd18802 5 VIPKLQKLIEILREYfpKTPDFRGIIFVERRATAVVLSRLLKEHPSTlafircgfligrgnsSQRKRSLMTQRKQKETLD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 334183955 316 RFRARKTMLLIVTDIAARGIDIPLLDNVINWDFPPRPKIFVHRVGRAARAG 366
Cdd:cd18802 85 KFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN 135
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
62-380 |
1.28e-06 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 51.68 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 62 ILSGVDVVAMARTGSGKTAAFLIP--MLEKLkqhvpqggvrALILSP----TRDLAEQtLKftkELGkftdLRVSLLVGG 135
Cdd:COG0514 29 VLAGRDALVVMPTGGGKSLCYQLPalLLPGL----------TLVVSPlialMKDQVDA-LR---AAG----IRAAFLNSS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 136 DSMEDQ---FEELTKG-PDVIIATPGRLM-----HLLSEVDdmtlrtVEYVVFDEA------------DSLfgmgfaeQL 194
Cdd:COG0514 91 LSAEERrevLRALRAGeLKLLYVAPERLLnprflELLRRLK------ISLFAIDEAhcisqwghdfrpDYR-------RL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 195 HQILTQLSeNRQTLLFSATlpsalaefAKA----------GLREPQLVR--LDVENkispdLKLSFLTVRPEEKYSALLY 262
Cdd:COG0514 158 GELRERLP-NVPVLALTAT--------ATPrvradiaeqlGLEDPRVFVgsFDRPN-----LRLEVVPKPPDDKLAQLLD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 263 LVREHisSDQQTLIFVSTKHHVEFVNSLFKLENIePSVCY-GDMDQDARKIHVSRFRARKTMLLIVTdIA-ARGIDIPLL 340
Cdd:COG0514 224 FLKEH--PGGSGIVYCLSRKKVEELAEWLREAGI-RAAAYhAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDV 299
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 334183955 341 DNVINWDFPPRPKIFVHRVGRAARAGRTGCAYSFVTPEDM 380
Cdd:COG0514 300 RFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDV 339
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
71-221 |
1.55e-06 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 52.23 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 71 MARTGSGKTAAFLIPMLEKL--------KQHVPQGGVRALILSPTRDLA---EQTLKF-----TKELGKFTDLRVSLLVG 134
Cdd:PRK09751 2 IAPTGSGKTLAAFLYALDRLfreggedtREAHKRKTSRILYISPIKALGtdvQRNLQIplkgiADERRRRGETEVNLRVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 135 ---GDSMEDQFEELTKGP-DVIIATPGRLMHLLSEVDDMTLRTVEYVVFDE----ADSLFGMGFAEQLHQILTQLSENRQ 206
Cdd:PRK09751 82 irtGDTPAQERSKLTRNPpDILITTPESLYLMLTSRARETLRGVETVIIDEvhavAGSKRGAHLALSLERLDALLHTSAQ 161
|
170
....*....|....*..
gi 334183955 207 TLLFSATLPSA--LAEF 221
Cdd:PRK09751 162 RIGLSATVRSAsdVAAF 178
|
|
| DEXHc_SKIV2L |
cd18027 |
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ... |
51-222 |
2.22e-06 |
|
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350785 [Multi-domain] Cd Length: 179 Bit Score: 48.80 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 51 PTPIQRKTMPLILSGVDVVAMARTGSGKT--AAFLIPMLEKlkqHVpqggVRALILSPTRDLAEQtlkftkelgKFTDLR 128
Cdd:cd18027 9 LDVFQKQAILHLEAGDSVFVAAHTSAGKTvvAEYAIALAQK---HM----TRTIYTSPIKALSNQ---------KFRDFK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 129 VSL----LVGGDSmedqfeELTKGPDVIIATPGRLMHLLSEVDDMtLRTVEYVVFDEADSLFGMGFAEQLHQILTQLSEN 204
Cdd:cd18027 73 NTFgdvgLITGDV------QLNPEASCLIMTTEILRSMLYNGSDV-IRDLEWVIFDEVHYINDAERGVVWEEVLIMLPDH 145
|
170
....*....|....*...
gi 334183955 205 RQTLLFSATLPSALaEFA 222
Cdd:cd18027 146 VSIILLSATVPNTV-EFA 162
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
71-281 |
7.59e-06 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 49.31 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 71 MARTGSGKTAAFLIPMLEKLKQHVPQGGVRALilsPTRDLAEQTLkftKELGKFTDLRVsLLVGGDSMEDQFEELTKGP- 149
Cdd:COG1203 153 TAPTGGGKTEAALLFALRLAAKHGGRRIIYAL---PFTSIINQTY---DRLRDLFGEDV-LLHHSLADLDLLEEEEEYEs 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 150 --------------DVIIAT------------PG--RLMHLLSevddmtlRTVeyVVFDEADSLfgmgFAEQLHQILTQL 201
Cdd:COG1203 226 earwlkllkelwdaPVVVTTidqlfeslfsnrKGqeRRLHNLA-------NSV--IILDEVQAY----PPYMLALLLRLL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 202 SE----NRQTLLFSATLPsalAEFAKAGLREPQLV--RLDVENKISPDLKLSFLTVRPEE-KYSALLYLVREHISSDQQT 274
Cdd:COG1203 293 EWlknlGGSVILMTATLP---PLLREELLEAYELIpdEPEELPEYFRAFVRKRVELKEGPlSDEELAELILEALHKGKSV 369
|
....*..
gi 334183955 275 LIFVSTK 281
Cdd:COG1203 370 LVIVNTV 376
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
63-181 |
1.11e-05 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 47.09 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 63 LSGVDVVAMARTGSGKT-AAFLIPM--LEKLKQHVPQGgvRALILSPTRDLAEQTLkfTKELGKFTDL-RVSLLVGGDSM 138
Cdd:cd18036 15 LRGKNTIICAPTGSGKTrVAVYICRhhLEKRRSAGEKG--RVVVLVNKVPLVEQQL--EKFFKYFRKGyKVTGLSGDSSH 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 334183955 139 EDQFEELTKGPDVIIATPGRLMHLL---SEVDDMTLRTVEYVVFDE 181
Cdd:cd18036 91 KVSFGQIVKASDVIICTPQILINNLlsgREEERVYLSDFSLLIFDE 136
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
62-226 |
1.26e-05 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 46.56 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 62 ILSGVDVVAMARTGSGKTaafLIPMLEKLKqHVPQGGvRALILSPTRDLAEQTLK-FTK--ELGkftdLRVSLLVGgdsM 138
Cdd:cd18028 14 LLKGENLLISIPTASGKT---LIAEMAMVN-TLLEGG-KALYLVPLRALASEKYEeFKKleEIG----LKVGISTG---D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 139 EDQFEELTKGPDVIIATPGRLMHLLSEVDDMtLRTVEYVVFDEADSLFGMGFAEQLHQILTQLSE---NRQTLLFSATLP 215
Cdd:cd18028 82 YDEDDEWLGDYDIIVATYEKFDSLLRHSPSW-LRDVGVVVVDEIHLISDEERGPTLESIVARLRRlnpNTQIIGLSATIG 160
|
170
....*....|...
gi 334183955 216 SA--LAEFAKAGL 226
Cdd:cd18028 161 NPdeLAEWLNAEL 173
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
256-364 |
1.34e-05 |
|
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: 45.81 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 256 KYSALLYLVREHI-----SSDQQTLIFVSTKHHV-EFVNSLFKL-ENIEPSVCYGD--------MDQDARKIHVSRFRAR 320
Cdd:cd18801 10 KLEKLEEIVKEHFkkkqeGSDTRVIIFSEFRDSAeEIVNFLSKIrPGIRATRFIGQasgksskgMSQKEQKEVIEQFRKG 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 334183955 321 KTMLLIVTDIAARGIDIPLLDNVINWDFPPRPKIFVHRVGRAAR 364
Cdd:cd18801 90 GYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
324-376 |
3.03e-05 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 42.69 E-value: 3.03e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 334183955 324 LLIVTDIAARGIDIPLLDNVINWDFPPRPKIFVHRVGRAARAGRTGCAYSFVT 376
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
63-182 |
3.06e-05 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 45.89 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 63 LSGVDVVAMARTGSGKTAAFLIPMLEKLKQHVPQGGVRALILSPTRDLAEQTL-KFTKELGKfTDLRVSLLVGGDSMEDQ 141
Cdd:cd17927 15 LKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGKVVFLANKVPLVEQQKeVFRKHFER-PGYKVTGLSGDTSENVS 93
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 334183955 142 FEELTKGPDVIIATPGRLMHLLSEVDDMTLRTVEYVVFDEA 182
Cdd:cd17927 94 VEQIVESSDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDEC 134
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
68-123 |
3.36e-05 |
|
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442728 [Multi-domain] Cd Length: 402 Bit Score: 47.29 E-value: 3.36e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 334183955 68 VVAMARTGSGKTAAFLIPMLEKLKQhvpqgGVRALILSPTRDLAEQTLKFTKELGK 123
Cdd:COG3505 2 VLVIGPTGSGKTVGLVIPNLTQLAR-----GESVVVTDPKGDLAELTAGFRRRAGY 52
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
274-364 |
4.48e-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: 43.32 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 274 TLIFVSTKHHVEFVNSLFKLENIEPSVCYGDMDQDAR---KIHVSRFRARKTMLLIVTDIAARGIDIPLLDNVInwdF-- 348
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgdeALILLFFGELKPPILVTVDLLTTGVDIPEVDNVV---Flr 85
|
90
....*....|....*..
gi 334183955 349 PPRPKI-FVHRVGRAAR 364
Cdd:cd18799 86 PTESRTlFLQMLGRGLR 102
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
68-213 |
5.88e-05 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 44.20 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 68 VVAMArTGSGKT--AAFLIpmLEKLKQHVPQggvRALILSPTRDLAEQTLK-FTKELGKftdlrvSLLVGGDSMEDQFEE 144
Cdd:pfam04851 27 LIVMA-TGSGKTltAAKLI--ARLFKKGPIK---KVLFLVPRKDLLEQALEeFKKFLPN------YVEIGEIISGDKKDE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 145 LTKGPDVIIATPGRLMHLLSEVDDMTLRT-VEYVVFDEADSLFGMGFAeqlhQILTQLSENRQtLLFSAT 213
Cdd:pfam04851 95 SVDDNKIVVTTIQSLYKALELASLELLPDfFDVIIIDEAHRSGASSYR----NILEYFKPAFL-LGLTAT 159
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
67-367 |
9.15e-05 |
|
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: 45.50 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 67 DVVAMARTGSGKTAAFLIPMLEKLKQHVPQGGVRALilsPTRDLAEQTLKFTKELGKFTDLRVSLLVGGDSM----EDQF 142
Cdd:cd09639 1 LLVIEAPTGYGKTEAALLWALHSLKSQKADRVIIAL---PTRATINAMYRRAKEAFGETGLYHSSILSSRIKemgdSEEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 143 EEL----TKGPDVIIATPGRLM---HLLSEV------DDMTLRTVEY--VVFDEADSL--FGMGFAEQLhqiLTQLSENR 205
Cdd:cd09639 78 EHLfplyIHSNDTLFLDPITVCtidQVLKSVfgefghYEFTLASIANslLIFDEVHFYdeYTLALILAV---LEVLKDND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 206 QT-LLFSATLPSALAEFAKAglrepqlvRLDVENKISPDLK---LSFLTVRPEEKYSALLYLVR--EHISSDQQTLIFVS 279
Cdd:cd09639 155 VPiLLMSATLPKFLKEYAEK--------IGYVEENEPLDLKpneRAPFIKIESDKVGEISSLERllEFIKKGGSVAIIVN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 280 T-KHHVEFVNSLFKLENIEPSVCY----GDMDQDARKIHVSRFRARKTMLLIV-TDIAARGIDIPLldNVINWDFPPrPK 353
Cdd:cd09639 227 TvDRAQEFYQQLKEKGPEEEIMLIhsrfTEKDRAKKEAELLLEFKKSEKFVIVaTQVIEASLDISV--DVMITELAP-ID 303
|
330
....*....|....
gi 334183955 354 IFVHRVGRAARAGR 367
Cdd:cd09639 304 SLIQRLGRLHRYGE 317
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
262-367 |
2.33e-04 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 42.24 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 262 YLVREHISSDQQTLIFVSTKHHVE----FVNSLFKLENIEPS--VCY--GDMDQDARKIHvSRFRARKTMLLIVTDIAAR 333
Cdd:cd18797 26 RLFADLVRAGVKTIVFCRSRKLAElllrYLKARLVEEGPLASkvASYraGYLAEDRREIE-AELFNGELLGVVATNALEL 104
|
90 100 110
....*....|....*....|....*....|....
gi 334183955 334 GIDIPLLDNVINWDFPPRPKIFVHRVGRAARAGR 367
Cdd:cd18797 105 GIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGK 138
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
256-366 |
2.57e-04 |
|
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: 41.69 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 256 KYSALLYLVREHISSDQQTLIFVstkHHVEFVNSL---FKLENIEPSVCYGDMDQDARKIHVSRFRA--RKTMLLIVTDI 330
Cdd:cd18793 12 KLEALLELLEELREPGEKVLIFS---QFTDTLDILeeaLRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIRVFLLSTKA 88
|
90 100 110
....*....|....*....|....*....|....*.
gi 334183955 331 AARGIDIPLLDNVINWDFPPRPKIFVHRVGRAARAG 366
Cdd:cd18793 89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIG 124
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
53-159 |
2.88e-04 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350773 [Multi-domain] Cd Length: 209 Bit Score: 43.12 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 53 PIQRKTMPLILSGVDVVAMARTGSGKTAAFLIPMLeklkqhvpQGGVRALILSPTRDLAEQTLKFTKELGkftdLRVSLL 132
Cdd:cd18015 21 PLQLETINATMAGRDVFLVMPTGGGKSLCYQLPAL--------CSDGFTLVVSPLISLMEDQLMALKKLG----ISATML 88
|
90 100 110
....*....|....*....|....*....|...
gi 334183955 133 VGGDSMEDQ---FEELTKGPD---VIIATPGRL 159
Cdd:cd18015 89 NASSSKEHVkwvHAALTDKNSelkLLYVTPEKI 121
|
|
| DEXHc_Mtr4-like |
cd18024 |
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or ... |
53-222 |
7.62e-04 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase Mtr4; Mtr4 (also known as DOB1 or SKIV2L2) is a type II DEAD box helicase that plays a role in the processing of structured RNAs, including the maturation of 5.8S ribosomal RNA (rRNA)and is part of the TRAMP complex that is involved in exosome-mediated degradation of aberrant RNAs. Mtr4 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: 350782 [Multi-domain] Cd Length: 205 Bit Score: 41.66 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 53 PIQRKTMPLILSGVDVVAMARTGSGKT--AAFLIPMLEKLKQhvpqggvRALILSPTRDLAEQtlKFTKELGKFTDlrVS 130
Cdd:cd18024 35 PFQKTAIACIERNESVLVSAHTSAGKTvvAEYAIAQSLRDKQ-------RVIYTSPIKALSNQ--KYRELQEEFGD--VG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 131 LLVGgdsmedqfeELTKGPD--VIIATPGRLMHLL---SEVddmtLRTVEYVVFDEA----DSLFGMGFAEQLhqILtqL 201
Cdd:cd18024 104 LMTG---------DVTINPNasCLVMTTEILRSMLyrgSEI----MREVAWVIFDEIhymrDKERGVVWEETI--IL--L 166
|
170 180
....*....|....*....|.
gi 334183955 202 SENRQTLLFSATLPSALaEFA 222
Cdd:cd18024 167 PDKVRYVFLSATIPNAR-QFA 186
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
46-156 |
1.74e-03 |
|
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350777 [Multi-domain] Cd Length: 214 Bit Score: 40.82 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 46 KGYKVPTPIQRKTMPLIL-SGVDVVAMARTGSGKTAAFLIPMLEKLKQHV-PQGGVRA-----LILSPTRDL-AEQTLKF 117
Cdd:cd18019 13 EGFKSLNRIQSKLFPAAFeTDENLLLCAPTGAGKTNVALLTILREIGKHRnPDGTINLdafkiVYIAPMKALvQEMVGNF 92
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 334183955 118 TKELgKFTDLRVSLLVGGDSM-EDQFEEltkgPDVIIATP 156
Cdd:cd18019 93 SKRL-APYGITVAELTGDQQLtKEQISE----TQIIVTTP 127
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
256-368 |
3.12e-03 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 40.98 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 256 KYSALLYLVREHISSDQQTLIFVSTKHHVEFVNSLFKLENIEPSVCYGDMDQDARKIHVSRFRARK--TMLLIVTDIAAR 333
Cdd:COG0553 534 KLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeaPVFLISLKAGGE 613
|
90 100 110
....*....|....*....|....*....|....*
gi 334183955 334 GIDIPLLDNVINWDFPPRPKIFVHRVGRAARAGRT 368
Cdd:COG0553 614 GLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQT 648
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
256-366 |
4.13e-03 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 40.87 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 256 KYSALLYLVREHISS--DQQTLIFVSTKHHVEFVNSLFKLENIEP------SVCYGD--MDQDARKIHVSRFRARKTMLL 325
Cdd:COG1111 336 KLSKLREILKEQLGTnpDSRIIVFTQYRDTAEMIVEFLSEPGIKAgrfvgqASKEGDkgLTQKEQIEILERFRAGEFNVL 415
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 334183955 326 IVTDIAARGIDIPLLDNVINWDFPPRPKIFVHRVGRAARAG 366
Cdd:COG1111 416 VATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGRKR 456
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
62-285 |
4.56e-03 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 40.71 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 62 ILSGVDVVAMARTGSGKTaafLIPMLEKLKQhVPQGGvRALILSPTRDLAEQtlKFTkELGKFTDLRVSllVG---GDSm 138
Cdd:PRK02362 36 LLDGKNLLAAIPTASGKT---LIAELAMLKA-IARGG-KALYIVPLRALASE--KFE-EFERFEELGVR--VGistGDY- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 139 eDQFEELTKGPDVIIATPGRLMHLL----SEVDDMTLrtveyVVFDEadslfgmgfaeqLHQI---------------LT 199
Cdd:PRK02362 105 -DSRDEWLGDNDIIVATSEKVDSLLrngaPWLDDITC-----VVVDE------------VHLIdsanrgptlevtlakLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 200 QLSENRQTLLFSATL--PSALAEFAKAGLRE----PQLVRLDV--ENKISPDLKLSFLTVRpeEKYSALlYLVREHISSD 271
Cdd:PRK02362 167 RLNPDLQVVALSATIgnADELADWLDAELVDsewrPIDLREGVfyGGAIHFDDSQREVEVP--SKDDTL-NLVLDTLEEG 243
|
250
....*....|....
gi 334183955 272 QQTLIFVSTKHHVE 285
Cdd:PRK02362 244 GQCLVFVSSRRNAE 257
|
|
| Cas3_I-D |
cd09710 |
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; ... |
68-301 |
6.48e-03 |
|
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; 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; Diverged DNA helicase Cas3'; signature gene for Type I and subtype I-D
Pssm-ID: 187841 [Multi-domain] Cd Length: 353 Bit Score: 39.85 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 68 VVAMARTGSGKTAAFLIPMLeklkqhvpQGGVRALILSPTRDLAEQTLKFTKELGKFTDLR---VSLLVGGDSMEDQFEE 144
Cdd:cd09710 17 IFNTAPTGAGKTLAWLTPLL--------HGENKAIALYPTNALIEDQTEAIKEFVDDANPRhqvKSLSASDITLWPNDKN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 145 --LTKG----------------------PDVIIATPGRLMHLLSEVDDMTLRTVEYVVFDE-----ADSLFGMGFAEQLH 195
Cdd:cd09710 89 vgSSKGeklynllrndigtstpiilltnPDIFVYLTRFAYIDRGDIAAGFYTKFSTVIFDEfhlydAKQLVGLLFYLAYM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 196 QILTQLSENRQTLLFSATLPSALAE-FAKAGLREPQLVRLDVE-------------------NKISPDLKLSFltvRPEE 255
Cdd:cd09710 169 QLIRFFECRRKFVFLSATPDPALILrLQNAKQAGVKIAPIDGEagqfpdnpeleqqlkntsfRPVLPPVELEL---IPAP 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 334183955 256 KYS-------ALLYLVREHISSDQQTLIFVSTKHHVEFVNSLFKLENIEPSVC 301
Cdd:cd09710 246 DFKeewlaelAAEVIERFRQLPGERGAIILDSLDEVNRLSDLLQQQGLGDDIG 298
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
75-182 |
7.09e-03 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 39.82 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 75 GSGKTaaflIPMLEKLKQHVPQGGV-RALILSPTrdlaeqTLKF--TKELGKFT-DLRVSLLVGGDSMEDQFEELtKGPD 150
Cdd:COG0553 270 GLGKT----IQALALLLELKERGLArPVLIVAPT------SLVGnwQRELAKFApGLRVLVLDGTRERAKGANPF-EDAD 338
|
90 100 110
....*....|....*....|....*....|...
gi 334183955 151 VIIATpgrlMHLL-SEVDDMTLRTVEYVVFDEA 182
Cdd:COG0553 339 LVITS----YGLLrRDIELLAAVDWDLVILDEA 367
|
|
| DEXHc_RE_I_III_res |
cd18032 |
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model ... |
69-182 |
8.29e-03 |
|
DEXH-box helicase domain of type III restriction enzyme res subunit; Members of this model includes both type I and type III restriction enzymes. Both are hetero-oligomeric proteins. Type I REs are encoded by three closely linked genes: a specificity subunit (HsdS or S) for recognizing a DNA sequence, a methylation subunit (HsdM or M) for methylating the recognized target bases, and a restriction subunit (HsdR or R) for the translocation and random cleavage of non-methylated DNA. They show diverse catalytic activities, including methyltransferase (MTase), ATP hydrolase (ATPase), DNA translocation and restriction activities. These enzymes cut at a site that differs, and is a random distance (at least 1000 bp) away, from their recognition site. Cleavage at these random sites follows a process of DNA translocation, which shows that these enzymes are also molecular motors. The recognition site is asymmetrical and is composed of two specific portions: one containing 3-4 nucleotides, and another containing 4-5 nucleotides, separated by a non-specific spacer of about 6-8 nucleotides. Type III enzymes are composed of two subunits, Res and Mod. The Mod subunit recognizes the DNA sequence specific for the system and is a modification methyltransferase; as such, it is functionally equivalent to the M and S subunits of type I restriction endonucleases. Res is required for restriction, although it has no enzymatic activity on its own. Type III enzymes recognize short 5-6 bp-long asymmetric DNA sequences and cleave 25-27 bp downstream to leave short, single-stranded 5' protrusions. They require the presence of two inversely oriented unmethylated recognition sites for restriction to occur. These enzymes methylate only one strand of the DNA, at the N-6 position of adenosyl residues, so newly replicated DNA will have only one strand methylated, which is sufficient to protect against restriction. Both type I and type III REs are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350790 [Multi-domain] Cd Length: 163 Bit Score: 37.93 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334183955 69 VAMArTGSGKT--AAFLIPMLekLKQHVPQggvRALILSPTRDLAEQTLKFTKELGKFTDLRVsLLVGGDSMEDQfeelt 146
Cdd:cd18032 25 LVMA-TGTGKTytAAFLIKRL--LEANRKK---RILFLAHREELLEQAERSFKEVLPDGSFGN-LKGGKKKPDDA----- 92
|
90 100 110
....*....|....*....|....*....|....*...
gi 334183955 147 kgpDVIIATPGRLMhllSEVDDMTLR--TVEYVVFDEA 182
Cdd:cd18032 93 ---RVVFATVQTLN---KRKRLEKFPpdYFDLIIIDEA 124
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
62-134 |
8.46e-03 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 39.52 E-value: 8.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334183955 62 ILSGVDVVAMARTGSGKTAAFLIPMLEklkqHVPQGGVRALILSPTRDLAEQ----TLKFTKELGKFtDLRVSLLVG 134
Cdd:COG1199 30 LAEGRHLLIEAGTGTGKTLAYLVPALL----AARETGKKVVISTATKALQEQlvekDLPLLRKALGL-PLRVALLKG 101
|
|
| |
