|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
1-332 |
9.65e-142 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 407.23 E-value: 9.65e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILEL-------GMKSLVVTPTRELTRQVA 73
Cdd:COG0513 9 LSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRldpsrprAPQALILAPTRELALQVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 74 SHIRDIGRYMDTKVAEVYGGMPYKAQINRV-RNADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKI 152
Cdd:COG0513 89 EELRKLAKYLGLRVATVYGGVSIGRQIRALkRGVDIVVATPGRLLDLIERGALDLSGVETLVLDEADRMLDMGFIEDIER 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 153 ILAQTSNRKITGLFSATIPEEIRKVVKDFITNYEEIEAC---IGLANVEHKFVHVKDdwRSKVQAL----RENKDKGVIV 225
Cdd:COG0513 169 ILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVApenATAETIEQRYYLVDK--RDKLELLrrllRDEDPERAIV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 226 FVRTRNRVAKLVRLFD----NAIELRGDLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKVINFDAPQDLRTYI 301
Cdd:COG0513 247 FCNTKRGADRLAEKLQkrgiSAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDYV 326
|
330 340 350
....*....|....*....|....*....|....*.
2Z0M_A 302 HRIGRTGRMGRKGEAITFILNEYW-----LEKEVKK 332
Cdd:COG0513 327 HRIGRTGRAGAEGTAISLVTPDERrllraIEKLIGQ 362
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
11-320 |
2.82e-88 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 272.44 E-value: 2.82e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 11 EMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILE------LGMKSLVVTPTRELTRQVASHIRDIGRYMD 84
Cdd:PRK11776 21 ELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQkldvkrFRVQALVLCPTRELADQVAKEIRRLARFIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 85 -TKVAEVYGGMPYKAQINRVRN-ADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIILAQTSNRKI 162
Cdd:PRK11776 101 nIKVLTLCGGVPMGPQIDSLEHgAHIIVGTPGRILDHLRKGTLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPARRQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 163 TGLFSATIPEEIRKVVKDFITNYEEI--EACIGLANVEHKFVHVKDDWRSKVQA--LRENKDKGVIVFVRTRNRVAKLVR 238
Cdd:PRK11776 181 TLLFSATYPEGIAAISQRFQRDPVEVkvESTHDLPAIEQRFYEVSPDERLPALQrlLLHHQPESCVVFCNTKKECQEVAD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 239 LFDN----AIELRGDLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKVINFDAPQDLRTYIHRIGRTGRMGRKG 314
Cdd:PRK11776 261 ALNAqgfsALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKG 340
|
....*.
2Z0M_A 315 EAITFI 320
Cdd:PRK11776 341 LALSLV 346
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
7-320 |
9.50e-88 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 270.28 E-value: 9.50e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 7 QAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILELGM-----KS-----LVVTPTRELTRQVASHI 76
Cdd:PRK11192 14 EALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLdfprrKSgppriLILTPTRELAMQVADQA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 77 RDIGRYMDTKVAEVYGGMPYKAQINRV-RNADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIILA 155
Cdd:PRK11192 94 RELAKHTHLDIATITGGVAYMNHAEVFsENQDIVVATPGRLLQYIKEENFDCRAVETLILDEADRMLDMGFAQDIETIAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 156 QTSNRKITGLFSATIP-EEIRKVVKDFITNYEEIEAciglanvE---------HKFVHVKDDWRSK----VQALRENKDK 221
Cdd:PRK11192 174 ETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEA-------EpsrrerkkiHQWYYRADDLEHKtallCHLLKQPEVT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 222 GVIVFVRTRNRVAKLV-RLFDNAIE---LRGDLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKVINFDAPQDL 297
Cdd:PRK11192 247 RSIVFVRTRERVHELAgWLRKAGINccyLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINFDMPRSA 326
|
330 340
....*....|....*....|...
2Z0M_A 298 RTYIHRIGRTGRMGRKGEAITFI 320
Cdd:PRK11192 327 DTYLHRIGRTGRAGRKGTAISLV 349
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
5-189 |
2.59e-85 |
|
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: 255.44 E-value: 2.59e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 5 IEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILEL----------GMKSLVVTPTRELTRQVAS 74
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKllpepkkkgrGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 75 HIRDIGRYMDTKVAEVYGGMPYKAQINRVRN-ADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKII 153
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKgPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRMLDMGFEEDVEKI 160
|
170 180 190
....*....|....*....|....*....|....*.
2Z0M_A 154 LAQTSNRKITGLFSATIPEEIRKVVKDFITNYEEIE 189
Cdd:cd00268 161 LSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
1-322 |
2.90e-75 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 243.22 E-value: 2.90e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPIL---ELGMKS---LVVTPTRELTRQVAS 74
Cdd:PRK11634 13 LKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnlDPELKApqiLVLAPTRELAVQVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 75 HIRDIGRYM-DTKVAEVYGGMPYKAQINRVRN-ADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKI 152
Cdd:PRK11634 93 AMTDFSKHMrGVNVVALYGGQRYDVQLRALRQgPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVET 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 153 ILAQTSNRKITGLFSATIPEEIRKVVKDFITNYEEIEAciglanveHKFVHVKDD-----WRskVQALRENKD------- 220
Cdd:PRK11634 173 IMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRI--------QSSVTTRPDisqsyWT--VWGMRKNEAlvrflea 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 221 ---KGVIVFVRTRN---RVAK-LVRLFDNAIELRGDLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKVINFDA 293
Cdd:PRK11634 243 edfDAAIIFVRTKNatlEVAEaLERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDI 322
|
330 340
....*....|....*....|....*....
2Z0M_A 294 PQDLRTYIHRIGRTGRMGRKGEAITFILN 322
Cdd:PRK11634 323 PMDSESYVHRIGRTGRAGRAGRALLFVEN 351
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
1-336 |
2.62e-71 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 228.54 E-value: 2.62e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILEL------------GMKSLVVTPTREL 68
Cdd:PRK10590 8 LSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHlitrqphakgrrPVRALILTPTREL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 69 TRQVASHIRDIGRYMDTKVAEVYGGMPYKAQINRVRNA-DIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFI 147
Cdd:PRK10590 88 AAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGvDVLVATPGRLLDLEHQNAVKLDQVEILVLDEADRMLDMGFI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 148 DDIKIILAQTSNRKITGLFSATIPEEIRKVVKDFITNYEEIEACIGLANVEH--KFVHVKDDWRSK---VQALRENKDKG 222
Cdd:PRK10590 168 HDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQvtQHVHFVDKKRKRellSQMIGKGNWQQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 223 VIVFVRTRNRVAKLVRLFD----NAIELRGDLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKVINFDAPQDLR 298
Cdd:PRK10590 248 VLVFTRTKHGANHLAEQLNkdgiRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPE 327
|
330 340 350
....*....|....*....|....*....|....*....
2Z0M_A 299 TYIHRIGRTGRMGRKGEAITFI-LNEYWLEKEVKKVSQK 336
Cdd:PRK10590 328 DYVHRIGRTGRAAATGEALSLVcVDEHKLLRDIEKLLKK 366
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
4-319 |
1.56e-69 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 224.41 E-value: 1.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 4 KIEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILE------------LG-MKSLVVTPTRELTR 70
Cdd:PRK01297 97 ELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINqllqtpppkeryMGePRALIIAPTRELVV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 71 QVASHIRDIGRYMDTKVAEVYGGMPYKAQINRV--RNADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFID 148
Cdd:PRK01297 177 QIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeaRFCDILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIP 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 149 DIKIILAQTSNR--KITGLFSATIPEEIRKVVKDFITN--YEEIEA-CIGLANVEHKFVHV--KDDWRSKVQALRENKDK 221
Cdd:PRK01297 257 QVRQIIRQTPRKeeRQTLLFSATFTDDVMNLAKQWTTDpaIVEIEPeNVASDTVEQHVYAVagSDKYKLLYNLVTQNPWE 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 222 GVIVFVRTRNRV----AKLVRLFDNAIELRGDLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKVINFDAPQDL 297
Cdd:PRK01297 337 RVMVFANRKDEVrrieERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDP 416
|
330 340
....*....|....*....|..
2Z0M_A 298 RTYIHRIGRTGRMGRKGEAITF 319
Cdd:PRK01297 417 DDYVHRIGRTGRAGASGVSISF 438
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
1-324 |
4.55e-64 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 208.67 E-value: 4.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAI---------PILELGM----KSLVVTPTRE 67
Cdd:PRK04837 15 LHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTatfhyllshPAPEDRKvnqpRALIMAPTRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 68 LTRQVASHIRDIGRYMDTKVAEVYGGMPYKAQINRVRN-ADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGF 146
Cdd:PRK04837 95 LAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESgVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMFDLGF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 147 IDDIKIILAQ--TSNRKITGLFSATIPEEIRKVVKDFITNYE----EIEACIGLANVEHKFVHVKDDWRSKVQALRENK- 219
Cdd:PRK04837 175 IKDIRWLFRRmpPANQRLNMLFSATLSYRVRELAFEHMNNPEyvevEPEQKTGHRIKEELFYPSNEEKMRLLQTLIEEEw 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 220 -DKgVIVFVRTRNRVAKL----------VRLfdnaieLRGDLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKV 288
Cdd:PRK04837 255 pDR-AIIFANTKHRCEEIwghlaadghrVGL------LTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHV 327
|
330 340 350
....*....|....*....|....*....|....*.
2Z0M_A 289 INFDAPQDLRTYIHRIGRTGRMGRKGEAITFILNEY 324
Cdd:PRK04837 328 FNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEY 363
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
5-337 |
9.09e-58 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 195.38 E-value: 9.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 5 IEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAY---------AIPILELGMKS--LVVTPTRELTRQVA 73
Cdd:PTZ00110 141 ILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFllpaivhinAQPLLRYGDGPivLVLAPTRELAEQIR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 74 SHIRDIGRYMDTKVAEVYGGMPYKAQINRVRN-ADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKI 152
Cdd:PTZ00110 221 EQCNKFGASSKIRNTVAYGGVPKRGQIYALRRgVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRK 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 153 ILAQTSNRKITGLFSATIPEEIRKVVKDFITNyEEIEACIG------LANVEhKFVHVKDDWRSKVQaLRE------NKD 220
Cdd:PTZ00110 301 IVSQIRPDRQTLMWSATWPKEVQSLARDLCKE-EPVHVNVGsldltaCHNIK-QEVFVVEEHEKRGK-LKMllqrimRDG 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 221 KGVIVFVRTR---NRVAKLVRLfDN--AIELRGDLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKVINFDAPQ 295
Cdd:PTZ00110 378 DKILIFVETKkgaDFLTKELRL-DGwpALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPN 456
|
330 340 350 360
....*....|....*....|....*....|....*....|...
2Z0M_A 296 DLRTYIHRIGRTGRMGRKGEAITFIL-NEYWLEKEVKKVSQKA 337
Cdd:PTZ00110 457 QIEDYVHRIGRTGRAGAKGASYTFLTpDKYRLARDLVKVLREA 499
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
13-324 |
1.39e-57 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 195.55 E-value: 1.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 13 GFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILELGM-------------KSLVVTPTRELTRQVASHIRDI 79
Cdd:PRK04537 28 GFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLsrpaladrkpedpRALILAPTRELAIQIHKDAVKF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 80 GRYMDTKVAEVYGGMPYKAQINRVRN-ADIVVATPGRLLD-LWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIILAQT 157
Cdd:PRK04537 108 GADLGLRFALVYGGVDYDKQRELLQQgVDVIIATPGRLIDyVKQHKVVSLHACEICVLDEADRMFDLGFIKDIRFLLRRM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 158 SNR--KITGLFSATIPEEIRKVVKDFITNYEEIEA---CIGLANVEHKFVHVKDDWRSKV--QALRENKDKGVIVFVRTR 230
Cdd:PRK04537 188 PERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVeteTITAARVRQRIYFPADEEKQTLllGLLSRSEGARTMVFVNTK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 231 NRVAKLVRLFDNAIE----LRGDLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKVINFDAPQDLRTYIHRIGR 306
Cdd:PRK04537 268 AFVERVARTLERHGYrvgvLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGR 347
|
330
....*....|....*...
2Z0M_A 307 TGRMGRKGEAITFILNEY 324
Cdd:PRK04537 348 TARLGEEGDAISFACERY 365
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
18-177 |
1.83e-56 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 180.90 E-value: 1.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 18 TEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILEL------GMKSLVVTPTRELTRQVASHIRDIGRYMDTKVAEVY 91
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAldkldnGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 92 GGMPYKAQINRVRNADIVVATPGRLLDLWSKGVIdLSSFEIVIIDEADLMFEMGFIDDIKIILAQTSNRKITGLFSATIP 171
Cdd:pfam00270 81 GGDSRKEQLEKLKGPDILVGTPGRLLDLLQERKL-LKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSATLP 159
|
....*.
2Z0M_A 172 EEIRKV 177
Cdd:pfam00270 160 RNLEDL 165
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
3-323 |
2.55e-54 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 185.76 E-value: 2.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 3 EKIEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILE----------------LGMkslVVTPTR 66
Cdd:PLN00206 130 PKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISrcctirsghpseqrnpLAM---VLTPTR 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 67 ELTRQVASHIRDIGRYMDTKVAEVYGGMPYKAQINRVRNA-DIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMG 145
Cdd:PLN00206 207 ELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGvELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERG 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 146 FIDDIKIILAQTSNRKITgLFSATIPEEIRKVVKDFITNYeeIEACIGLANVEHKFVHVKDDW---RSKVQAL------R 216
Cdd:PLN00206 287 FRDQVMQIFQALSQPQVL-LFSATVSPEVEKFASSLAKDI--ILISIGNPNRPNKAVKQLAIWvetKQKKQKLfdilksK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 217 ENKDKGVIVFVRTR-------NRVAKLVRLfdNAIELRGDLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKVI 289
Cdd:PLN00206 364 QHFKPPAVVFVSSRlgadllaNAITVVTGL--KALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVI 441
|
330 340 350
....*....|....*....|....*....|....
2Z0M_A 290 NFDAPQDLRTYIHRIGRTGRMGRKGEAITFILNE 323
Cdd:PLN00206 442 IFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEE 475
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
8-179 |
1.05e-52 |
|
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: 172.44 E-value: 1.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 8 AIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILEL---------GMKSLVVTPTRELTRQVASHIRD 78
Cdd:cd17947 4 ALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERllyrpkkkaATRVLVLVPTRELAMQCFSVLQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 79 IGRYMDTKVAEVYGGMPYKAQINRVR-NADIVVATPGRLLDLW--SKGViDLSSFEIVIIDEADLMFEMGFIDDIKIILA 155
Cdd:cd17947 84 LAQFTDITFALAVGGLSLKAQEAALRaRPDIVIATPGRLIDHLrnSPSF-DLDSIEILVLDEADRMLEEGFADELKEILR 162
|
170 180
....*....|....*....|....
2Z0M_A 156 QTSNRKITGLFSATIPEEIRKVVK 179
Cdd:cd17947 163 LCPRTRQTMLFSATMTDEVKDLAK 186
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
8-188 |
1.84e-52 |
|
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350717 [Multi-domain] Cd Length: 205 Bit Score: 172.10 E-value: 1.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 8 AIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILEL--------GMKSLVVTPTRELTRQVASHIRDI 79
Cdd:cd17959 15 AIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKlkahsptvGARALILSPTRELALQTLKVTKEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 80 GRYMDTKVAEVYGGMPYKAQINRV-RNADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIILAQTS 158
Cdd:cd17959 95 GKFTDLRTALLVGGDSLEEQFEALaSNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDEADRLFEMGFAEQLHEILSRLP 174
|
170 180 190
....*....|....*....|....*....|
2Z0M_A 159 NRKITGLFSATIPEEIRKVVKDFITNYEEI 188
Cdd:cd17959 175 ENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
2-176 |
7.42e-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: 170.46 E-value: 7.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 2 NEKIEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILEL------------GMKSLVVTPTRELT 69
Cdd:cd17961 2 DPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKilkakaesgeeqGTRALILVPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 70 RQVASHIRDIGRYM--DTKVAEVYGGMPYKAQINRVR-NADIVVATPGRLLDLWSKGVI-DLSSFEIVIIDEADLMFEMG 145
Cdd:cd17961 82 QQVSKVLEQLTAYCrkDVRVVNLSASSSDSVQRALLAeKPDIVVSTPARLLSHLESGSLlLLSTLKYLVIDEADLVLSYG 161
|
170 180 190
....*....|....*....|....*....|.
2Z0M_A 146 FIDDIKIILAQTSNRKITGLFSATIPEEIRK 176
Cdd:cd17961 162 YEEDLKSLLSYLPKNYQTFLMSATLSEDVEA 192
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
5-179 |
1.49e-50 |
|
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: 166.98 E-value: 1.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 5 IEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILEL-----------GMKSLVVTPTRELTRQVA 73
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEIllkrkanlkkgQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 74 SHIRDIGRYMDTKVAE--VYGGMPYKAQINRVRN--ADIVVATPGRLLDLWS--KGVIDLSSFEIVIIDEADLMFEMGFI 147
Cdd:cd17960 81 EVLQSFLEHHLPKLKCqlLIGGTNVEEDVKKFKRngPNILVGTPGRLEELLSrkADKVKVKSLEVLVLDEADRLLDLGFE 160
|
170 180 190
....*....|....*....|....*....|..
2Z0M_A 148 DDIKIILAQTSNRKITGLFSATIPEEIRKVVK 179
Cdd:cd17960 161 ADLNRILSKLPKQRRTGLFSATQTDAVEELIK 192
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
1-323 |
4.01e-50 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 171.93 E-value: 4.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILEL------GMKSLVVTPTRELTRQVAS 74
Cdd:PTZ00424 35 LNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLidydlnACQALILAPTRELAQQIQK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 75 HIRDIGRYMDTKVAEVYGGMPYKAQINRVRNA-DIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKII 153
Cdd:PTZ00424 115 VVLALGDYLKVRCHACVGGTVVRDDINKLKAGvHMVVGTPGRVYDMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 154 LAQTSNRKITGLFSATIPEEIRKVVKDFITNYEEI---EACIGLANVEHKFVHV-KDDWrsKVQALRENKDK----GVIV 225
Cdd:PTZ00424 195 FKKLPPDVQVALFSATMPNEILELTTKFMRDPKRIlvkKDELTLEGIRQFYVAVeKEEW--KFDTLCDLYETltitQAII 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 226 FVRTRNRVAKLVRLFDNAI----ELRGDLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKVINFDAPQDLRTYI 301
Cdd:PTZ00424 273 YCNTRRKVDYLTKKMHERDftvsCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYI 352
|
330 340
....*....|....*....|..
2Z0M_A 302 HRIGRTGRMGRKGEAITFILNE 323
Cdd:PTZ00424 353 HRIGRSGRFGRKGVAINFVTPD 374
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
197-320 |
7.47e-49 |
|
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: 159.98 E-value: 7.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 197 VEHKFVHVKDDWRSK---VQALRENKDKGVIVFVRTRNRVAKLVRLFDN----AIELRGDLPQSVRNRNIDAFREGEYDM 269
Cdd:cd18787 1 IKQLYVVVEEEEKKLlllLLLLEKLKPGKAIIFVNTKKRVDRLAELLEElgikVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
2Z0M_A 270 LITTDVASRGLDIPLVEKVINFDAPQDLRTYIHRIGRTGRMGRKGEAITFI 320
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
1-179 |
2.41e-48 |
|
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350722 [Multi-domain] Cd Length: 211 Bit Score: 161.60 E-value: 2.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREMGFKNFTEVQSKTIPLMLQ-GKNVVVRAKTGSGKTAAYAIPILE-----------LGMKSLVVTPTREL 68
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQsllntkpagrrSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 69 TRQVASHIRDIGRYM-DTKVAEVYGGMPYKAQINRVR--NADIVVATPGRLLDLWS--KGVIDLSSFEIVIIDEADLMFE 143
Cdd:cd17964 81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLRrgRPDILVATPGRLIDHLEnpGVAKAFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
2Z0M_A 144 MGFIDDIKIILAQTSNRKITG----LFSATIPEEIRKVVK 179
Cdd:cd17964 161 MGFRPDLEQILRHLPEKNADPrqtlLFSATVPDEVQQIAR 200
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
9-188 |
2.58e-48 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 161.12 E-value: 2.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 9 IREMGFKNFTEVQSKTIPLMLQG-KNVVVRAKTGSGKTAAYAIPILELGMKS-----LVVTPTRELTRQVASHIRDIGRY 82
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGkggrvLVLVPTRELAEQWAEELKKLGPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 83 MDTKVAEVYGGMPYKAQINRVRN--ADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIILAQTSNR 160
Cdd:smart00487 81 LGLKVVGLYGGDSKREQLRKLESgkTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKN 160
|
170 180
....*....|....*....|....*...
2Z0M_A 161 KITGLFSATIPEEIRKVVKDFITNYEEI 188
Cdd:smart00487 161 VQLLLLSATPPEEIENLLELFLNDPVFI 188
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
9-182 |
2.94e-48 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 160.83 E-value: 2.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 9 IREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPIL--------ELGMKSLVVTPTRELTRQVASHIRDIG 80
Cdd:cd17957 5 LEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILqklgkprkKKGLRALILAPTRELASQIYRELLKLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 81 RYMDTKVAEVYGGMPYKAQINRV--RNADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIILAQTS 158
Cdd:cd17957 85 KGTGLRIVLLSKSLEAKAKDGPKsiTKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLFEPGFREQTDEILAACT 164
|
170 180
....*....|....*....|....*....
2Z0M_A 159 NRKIT-GLFSATIPEEI----RKVVKDFI 182
Cdd:cd17957 165 NPNLQrSLFSATIPSEVeelaRSVMKDPI 193
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
9-188 |
1.09e-47 |
|
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: 159.39 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 9 IREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILE------LGMKSLVVTPTRELTRQVASHIRDIGRY 82
Cdd:cd17940 14 IFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEkidpkkDVIQALILVPTRELALQTSQVCKELGKH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 83 MDTKVAEVYGGMPYKAQINRVRNA-DIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIILAQTSNRK 161
Cdd:cd17940 94 MGVKVMVTTGGTSLRDDIMRLYQTvHVLVGTPGRILDLAKKGVADLSHCKTLVLDEADKLLSQDFQPIIEKILNFLPKER 173
|
170 180
....*....|....*....|....*..
2Z0M_A 162 ITGLFSATIPEEIRKVVKDFITNYEEI 188
Cdd:cd17940 174 QILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
1-185 |
1.65e-45 |
|
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: 154.57 E-value: 1.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILELGMKS----------------LVVTP 64
Cdd:cd17967 7 LRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDgppsvgrgrrkaypsaLILAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 65 TRELtrqvASHIRDIGR---YmDT--KVAEVYGGMPYKAQINRV-RNADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEA 138
Cdd:cd17967 87 TREL----AIQIYEEARkfsY-RSgvRSVVVYGGADVVHQQLQLlRGCDILVATPGRLVDFIERGRISLSSIKFLVLDEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
2Z0M_A 139 DLMFEMGFIDDIKIILAQTS-----NRkITGLFSATIPEEIRKVVKDFITNY 185
Cdd:cd17967 162 DRMLDMGFEPQIRKIVEHPDmppkgER-QTLMFSATFPREIQRLAADFLKNY 212
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
5-188 |
3.12e-44 |
|
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: 150.52 E-value: 3.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 5 IEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILEL----------GMKSLVVTPTRELTRQVAS 74
Cdd:cd17941 1 TLKGLKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKlyrerwtpedGLGALIISPTRELAMQIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 75 HIRDIGRYMDTKVAEVYGGMPYKAQINRVRNADIVVATPGRLLDLWSKGV-IDLSSFEIVIIDEADLMFEMGFIDDIKII 153
Cdd:cd17941 81 VLRKVGKYHSFSAGLIIGGKDVKEEKERINRMNILVCTPGRLLQHMDETPgFDTSNLQMLVLDEADRILDMGFKETLDAI 160
|
170 180 190
....*....|....*....|....*....|....*
2Z0M_A 154 LAQTSNRKITGLFSATIPEEIRKVVKDFITNYEEI 188
Cdd:cd17941 161 VENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYI 195
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
7-177 |
3.37e-43 |
|
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: 147.76 E-value: 3.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 7 QAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILE------LGMKSLVVTPTRELTRQVASHIRDIG 80
Cdd:cd17955 12 KQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQrlsedpYGIFALVLTPTRELAYQIAEQFRALG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 81 RYMDTKVAEVYGGMPYKAQINRVRN-ADIVVATPGRLLDLW---SKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIILAQ 156
Cdd:cd17955 92 APLGLRCCVIVGGMDMVKQALELSKrPHIVVATPGRLADHLrssDDTTKVLSRVKFLVLDEADRLLTGSFEDDLATILSA 171
|
170 180
....*....|....*....|.
2Z0M_A 157 TSNRKITGLFSATIPEEIRKV 177
Cdd:cd17955 172 LPPKRQTLLFSATLTDALKAL 192
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
1-185 |
1.41e-42 |
|
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: 148.19 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILELGMKS---------------LVVTPT 65
Cdd:cd18052 50 LCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgltassfsevqepqaLIVAPT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 66 RELTRQVASHIRDIGRYMDTKVAEVYGGMPYKAQINRV-RNADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEM 144
Cdd:cd18052 130 RELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIeKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDM 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
2Z0M_A 145 GFIDDIKIILAQTS----NRKITGLFSATIPEEIRKVVKDFI-TNY 185
Cdd:cd18052 210 GFGPEIRKLVSEPGmpskEDRQTLMFSATFPEEIQRLAAEFLkEDY 255
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
9-188 |
1.72e-42 |
|
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: 145.98 E-value: 1.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 9 IREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPIL-----------ELGMKSLVVTPTRELTRQVASHIR 77
Cdd:cd17966 5 LKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvhinaqpplerGDGPIVLVLAPTRELAQQIQQEAN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 78 DIGRYMDTKVAEVYGGMPYKAQINRV-RNADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIILAQ 156
Cdd:cd17966 85 KFGGSSRLRNTCVYGGAPKGPQIRDLrRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADRMLDMGFEPQIRKIVDQ 164
|
170 180 190
....*....|....*....|....*....|..
2Z0M_A 157 TSNRKITGLFSATIPEEIRKVVKDFITNYEEI 188
Cdd:cd17966 165 IRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
1-176 |
6.48e-41 |
|
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: 142.07 E-value: 6.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILE------LGMKSLVVTPTRELTRQVAS 74
Cdd:cd17954 7 VCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQallenpQRFFALVLAPTRELAQQISE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 75 HIRDIGRYMDTKVAEVYGGMPYKAQ-INRVRNADIVVATPGRLLDLW--SKGViDLSSFEIVIIDEADLMFEMGFIDDIK 151
Cdd:cd17954 87 QFEALGSSIGLKSAVLVGGMDMMAQaIALAKKPHVIVATPGRLVDHLenTKGF-SLKSLKFLVMDEADRLLNMDFEPEID 165
|
170 180
....*....|....*....|....*
2Z0M_A 152 IILAQTSNRKITGLFSATIPEEIRK 176
Cdd:cd17954 166 KILKVIPRERTTYLFSATMTTKVAK 190
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
1-188 |
2.36e-40 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350711 [Multi-domain] Cd Length: 222 Bit Score: 140.98 E-value: 2.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPIL-----------ELGMKSLVVTPTRELT 69
Cdd:cd17953 19 LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFrhikdqrpvkpGEGPIGLIMAPTRELA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 70 RQVASHIRDIGRYMDTKVAEVYGGMPYKAQINRV-RNADIVVATPGRLLDLWSKG---VIDLSSFEIVIIDEADLMFEMG 145
Cdd:cd17953 99 LQIYVECKKFSKALGLRVVCVYGGSGISEQIAELkRGAEIVVCTPGRMIDILTANngrVTNLRRVTYVVLDEADRMFDMG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
2Z0M_A 146 FIDDIKIILAQTSNRKITGLFSATIPEEIRKVVKDFITNYEEI 188
Cdd:cd17953 179 FEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
3-189 |
6.84e-40 |
|
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: 139.40 E-value: 6.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 3 EKIEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILEL------GMKSLVVTPTRELTRQVASHI 76
Cdd:cd17950 11 PELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQlepvdgQVSVLVICHTRELAFQISNEY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 77 RDIGRYM-DTKVAEVYGGMPYKAQINRVRNA--DIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMgfID---DI 150
Cdd:cd17950 91 ERFSKYMpNVKTAVFFGGVPIKKDIEVLKNKcpHIVVGTPGRILALVREKKLKLSHVKHFVLDECDKMLEQ--LDmrrDV 168
|
170 180 190
....*....|....*....|....*....|....*....
2Z0M_A 151 KIILAQTSNRKITGLFSATIPEEIRKVVKDFITNYEEIE 189
Cdd:cd17950 169 QEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIF 207
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
8-177 |
2.12e-39 |
|
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: 137.88 E-value: 2.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 8 AIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILEL----------GMKSLVVTPTRELTRQVASHIR 77
Cdd:cd17942 4 AIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELlyklkfkprnGTGVIIISPTRELALQIYGVAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 78 DIGRYMDTKVAEVYGGMPYKAQINRVRNA-DIVVATPGRLLD-LWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIILA 155
Cdd:cd17942 84 ELLKYHSQTFGIVIGGANRKAEAEKLGKGvNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQIIK 163
|
170 180
....*....|....*....|..
2Z0M_A 156 QTSNRKITGLFSATipeEIRKV 177
Cdd:cd17942 164 LLPKRRQTMLFSAT---QTRKV 182
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
7-184 |
5.45e-39 |
|
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: 136.78 E-value: 5.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 7 QAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPIL-------EL----GMKSLVVTPTRELTRQVASH 75
Cdd:cd17952 3 NAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLvhimdqrELekgeGPIAVIVAPTRELAQQIYLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 76 IRDIGRYMDTKVAEVYGGMPYKAQINRVR-NADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIIL 154
Cdd:cd17952 83 AKKFGKAYNLRVVAVYGGGSKWEQAKALQeGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDMGFEYQVRSIV 162
|
170 180 190
....*....|....*....|....*....|
2Z0M_A 155 AQTSNRKITGLFSATIPEEIRKVVKDFITN 184
Cdd:cd17952 163 GHVRPDRQTLLFSATFKKKIEQLARDILSD 192
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
5-183 |
8.23e-39 |
|
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350696 [Multi-domain] Cd Length: 204 Bit Score: 136.68 E-value: 8.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 5 IEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILELgMKSLVVTPTRELTRQVASHIRDIGRYMD 84
Cdd:cd17938 10 LIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQI-VVALILEPSRELAEQTYNCIENFKKYLD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 85 T---KVAEVYGGMPYKAQINRVRN-ADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIILAQTSNR 160
Cdd:cd17938 89 NpklRVALLIGGVKAREQLKRLESgVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLDEADRLLSQGNLETINRIYNRIPKI 168
|
170 180 190
....*....|....*....|....*....|
2Z0M_A 161 KITG------LFSATI-PEEIRKVVkDFIT 183
Cdd:cd17938 169 TSDGkrlqviVCSATLhSFEVKKLA-DKIM 197
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
8-179 |
8.31e-39 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350703 [Multi-domain] Cd Length: 220 Bit Score: 137.07 E-value: 8.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 8 AIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPIL--------------ELGMKSLVVTPTRELTRQVA 73
Cdd:cd17945 4 VIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLvyisrlppldeetkDDGPYALILAPTRELAQQIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 74 SHIRDIGRYMDTKVAEVYGGMPYKAQINRVRN-ADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKI 152
Cdd:cd17945 84 EETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNgCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDMGFEPQVTK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
2Z0M_A 153 ILAQ--TSNRKI------------------TGLFSATIPEEIRKVVK 179
Cdd:cd17945 164 ILDAmpVSNKKPdteeaeklaasgkhryrqTMMFTATMPPAVEKIAK 210
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
20-189 |
8.99e-39 |
|
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: 136.52 E-value: 8.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 20 VQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILE------------LGMKSLVVTPTRELTRQVASHIRDIGRYMdtKV 87
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEklqedqqprkrgRAPKVLVLAPTRELANQVTKDFKDITRKL--SV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 88 AEVYGGMPYKAQINRVRNA-DIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIIL-----AQTSNRK 161
Cdd:cd17944 94 ACFYGGTPYQQQIFAIRNGiDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILsvsykKDSEDNP 173
|
170 180
....*....|....*....|....*....
2Z0M_A 162 ITGLFSATIPEEIRKVVKDFI-TNYEEIE 189
Cdd:cd17944 174 QTLLFSATCPDWVYNVAKKYMkSQYEQVD 202
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
5-170 |
4.85e-38 |
|
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: 135.44 E-value: 4.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 5 IEQAIREMGFKNFTEVQSKTIPL-MLQGKNVVVRAKTGSGKTAAYAIPILE---------------LGMKSLVVTPTREL 68
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILErllsqkssngvggkqKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 69 TRQVASHIRDIGRYMDTKVAEVYGGMPYKAQiNRV--RNADIVVATPGRLLDLWSKGVIDLSSFEIV---IIDEADLMFE 143
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKIASIVGGLAVQKQ-ERLlkKRPEIVVATPGRLWELIQEGNEHLANLKSLrflVLDEADRMLE 159
|
170 180 190
....*....|....*....|....*....|....
2Z0M_A 144 MGFIDDIKIILA------QTSNRKI-TGLFSATI 170
Cdd:cd17946 160 KGHFAELEKILEllnkdrAGKKRKRqTFVFSATL 193
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
9-184 |
8.77e-38 |
|
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: 133.44 E-value: 8.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 9 IREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILELGMK------SLVVTPTRELTRQVASHIRDIGR- 81
Cdd:cd17962 5 LKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTehrnpsALILTPTRELAVQIEDQAKELMKg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 82 YMDTKVAEVYGGMPYKAQINRVR-NADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIILAQTSNR 160
Cdd:cd17962 85 LPPMKTALLVGGLPLPPQLYRLQqGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHD 164
|
170 180
....*....|....*....|....
2Z0M_A 161 KITGLFSATIPEEIRKVVKDFITN 184
Cdd:cd17962 165 HQTILVSATIPRGIEQLAGQLLQN 188
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
12-179 |
6.65e-36 |
|
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: 129.24 E-value: 6.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 12 MGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILELGMKS------------LVVTPTRELTRQVASHIRDI 79
Cdd:cd17949 9 MGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLeprvdrsdgtlaLVLVPTRELALQIYEVLEKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 80 GRYMDTKV-AEVYGGMPYKAQINRVRN-ADIVVATPGRLLD-LWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIIL-- 154
Cdd:cd17949 89 LKPFHWIVpGYLIGGEKRKSEKARLRKgVNILIATPGRLLDhLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILel 168
|
170 180 190
....*....|....*....|....*....|....*.
2Z0M_A 155 --AQTSN---------RKITGLFSATIPEEIRKVVK 179
Cdd:cd17949 169 ldDKRSKaggekskpsRRQTVLVSATLTDGVKRLAG 204
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
14-188 |
3.84e-35 |
|
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: 128.98 E-value: 3.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 14 FKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPI---------LELGMKS--LVVTPTRELTRQVASHIRDIGRY 82
Cdd:cd18050 82 FKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAivhinhqpyLERGDGPicLVLAPTRELAQQVQQVADDYGKS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 83 MDTKVAEVYGGMPYKAQINRV-RNADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIILAQTSNRK 161
Cdd:cd18050 162 SRLKSTCIYGGAPKGPQIRDLeRGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDR 241
|
170 180
....*....|....*....|....*..
2Z0M_A 162 ITGLFSATIPEEIRKVVKDFITNYEEI 188
Cdd:cd18050 242 QTLMWSATWPKEVRQLAEDFLRDYVQI 268
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
5-184 |
7.96e-35 |
|
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: 126.04 E-value: 7.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 5 IEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPIL------------ELGMKSLVVTPTRELTRQV 72
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFihldlqpipreqRNGPGVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 73 ASHIRDIgRYMDTKVAEVYGGMPYKAQINRVRN-ADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIK 151
Cdd:cd17958 81 EAECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKgVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRMLDMGFEPQIR 159
|
170 180 190
....*....|....*....|....*....|...
2Z0M_A 152 IILAQTSNRKITGLFSATIPEEIRKVVKDFITN 184
Cdd:cd17958 160 KILLDIRPDRQTIMTSATWPDGVRRLAQSYLKD 192
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
1-188 |
1.10e-34 |
|
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: 125.51 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPIL------ELGMKSLVVTPTRELTRQVAS 74
Cdd:cd17939 4 LSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALqridttVRETQALVLAPTRELAQQIQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 75 HIRDIGRYMDTKVAEVYGGMPYKAQINRVR-NADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKII 153
Cdd:cd17939 84 VVKALGDYMGVKVHACIGGTSVREDRRKLQyGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDI 163
|
170 180 190
....*....|....*....|....*....|....*.
2Z0M_A 154 LaQTSNRKIT-GLFSATIPEEIRKVVKDFITNYEEI 188
Cdd:cd17939 164 F-QFLPPETQvVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
8-185 |
4.09e-34 |
|
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: 123.91 E-value: 4.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 8 AIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILE------LGMKSLVVTPTRELTRQVASHIRDIGR 81
Cdd:cd17943 4 GLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALEsldlerRHPQVLILAPTREIAVQIHDVFKKIGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 82 YMDTKVAEVY-GGMPYKAQINRVRNADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIILAQTSNR 160
Cdd:cd17943 84 KLEGLKCEVFiGGTPVKEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSSLPKN 163
|
170 180
....*....|....*....|....*
2Z0M_A 161 KITGLFSATIPEEIRKVVKDFITNY 185
Cdd:cd17943 164 KQVIAFSATYPKNLDNLLARYMRKP 188
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
7-188 |
4.54e-34 |
|
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, G17P1, or HUMP68) is involved in pathways that include the alteration of RNA structures, plays a role as a coregulator of transcription, a regulator of splicing, and in the processing of small noncoding RNAs. It synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. Dysregulation of this gene may play a role in cancer development. DDX5 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350807 [Multi-domain] Cd Length: 234 Bit Score: 125.12 E-value: 4.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 7 QAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIP---------ILELGMKS--LVVTPTRELTRQVASH 75
Cdd:cd18049 37 DVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPaivhinhqpFLERGDGPicLVLAPTRELAQQVQQV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 76 IRDIGRYMDTKVAEVYGGMPYKAQINRV-RNADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIIL 154
Cdd:cd18049 117 AAEYGRACRLKSTCIYGGAPKGPQIRDLeRGVEICIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIV 196
|
170 180 190
....*....|....*....|....*....|....
2Z0M_A 155 AQTSNRKITGLFSATIPEEIRKVVKDFITNYEEI 188
Cdd:cd18049 197 DQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHI 230
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
7-188 |
8.32e-34 |
|
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: 123.07 E-value: 8.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 7 QAIREMGFKNFTEVQSKTIPLMLQG--KNVVVRAKTGSGKTAAYAipileLGMKS-----------LVVTPTRELTRQVA 73
Cdd:cd17963 7 KGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFV-----LAMLSrvdptlkspqaLCLAPTRELARQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 74 SHIRDIGRYMDTKVA------EVYGGMPYKAQInrvrnadiVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEM-GF 146
Cdd:cd17963 82 EVVEKMGKFTGVKVAlavpgnDVPRGKKITAQI--------VIGTPGTVLDWLKKRQLDLKKIKILVLDEADVMLDTqGH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
2Z0M_A 147 IDDIKIIL-AQTSNRKITgLFSATIPEEIRKVVKDFITNYEEI 188
Cdd:cd17963 154 GDQSIRIKrMLPRNCQIL-LFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
18-185 |
8.69e-32 |
|
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: 119.37 E-value: 8.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 18 TEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPIL----ELG--------------MK----SLVVTPTRELTRQVASH 75
Cdd:cd18051 45 TPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILsqiyEQGpgeslpsesgyygrRKqyplALVLAPTRELASQIYDE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 76 IRDIGRYMDTKVAEVYGGMPYKAQINRV-RNADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIIL 154
Cdd:cd18051 125 ARKFAYRSRVRPCVVYGGADIGQQMRDLeRGCHLLVATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIV 204
|
170 180 190
....*....|....*....|....*....|....*.
2Z0M_A 155 AQ-----TSNRKiTGLFSATIPEEIRKVVKDFITNY 185
Cdd:cd18051 205 EQdtmppTGERQ-TLMFSATFPKEIQMLARDFLDNY 239
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
7-202 |
8.95e-32 |
|
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: 119.01 E-value: 8.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 7 QAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILE--LGMK-----------SLVVTPTRELTRQVA 73
Cdd:cd17948 3 EILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQrlLRYKllaegpfnaprGLVITPSRELAEQIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 74 SHIRDIGRYMDTKVAEVYGGMPYKAQINRVR-NADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKI 152
Cdd:cd17948 83 SVAQSLTEGLGLKVKVITGGRTKRQIRNPHFeEVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSH 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2Z0M_A 153 ILAQT---SNRK--ITG--------LFSATIPEEIRKVVKDfITNYEEIEACIG------LANVEHKFV 202
Cdd:cd17948 163 FLRRFplaSRRSenTDGldpgtqlvLVSATMPSGVGEVLSK-VIDVDSIETVTSdklhrlMPHVKQKFL 230
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
5-179 |
2.16e-31 |
|
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: 117.05 E-value: 2.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 5 IEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPI----LELGMK----------SLVVTPTRELTR 70
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLimfaLEQEKKlpfikgegpyGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 71 Q---VASHIR---DIGRYMDTKVAEVYGGMPYKAQINRVRNA-DIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFE 143
Cdd:cd17951 81 QtheVIEYYCkalQEGGYPQLRCLLCIGGMSVKEQLEVIRKGvHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMID 160
|
170 180 190
....*....|....*....|....*....|....*.
2Z0M_A 144 MGFIDDIKIILAQTSNRKITGLFSATIPEEIRKVVK 179
Cdd:cd17951 161 MGFEEDIRTIFSYFKGQRQTLLFSATMPKKIQNFAK 196
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
1-184 |
8.53e-28 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 107.53 E-value: 8.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPIL---ELGMK---SLVVTPTRELTRQVAS 74
Cdd:cd18046 6 LKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILqqiDTSLKatqALVLAPTRELAQQIQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 75 HIRDIGRYMDTKVAEVYGGMPYKAQINRVRNA-DIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKII 153
Cdd:cd18046 86 VVMALGDYMGIKCHACIGGTSVRDDAQKLQAGpHIVVGTPGRVFDMINRRYLRTDYIKMFVLDEADEMLSRGFKDQIYDI 165
|
170 180 190
....*....|....*....|....*....|.
2Z0M_A 154 LAQTSNRKITGLFSATIPEEIRKVVKDFITN 184
Cdd:cd18046 166 FQKLPPDTQVVLLSATMPNDVLEVTTKFMRD 196
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
212-311 |
6.60e-27 |
|
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: 102.29 E-value: 6.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 212 VQALRENKDKGVIVFVRTRNRVAK---LVRLFDNAIELRGDLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKV 288
Cdd:pfam00271 7 LELLKKERGGKVLIFSQTKKTLEAellLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDVDLV 86
|
90 100
....*....|....*....|...
2Z0M_A 289 INFDAPQDLRTYIHRIGRTGRMG 311
Cdd:pfam00271 87 INYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
7-174 |
1.38e-26 |
|
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: 105.02 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 7 QAIREMGFKNFTEVQSKTIPLMLQG---------KNVVVRAKTGSGKTAAYAIPILEL-------GMKSLVVTPTRELTR 70
Cdd:cd17956 3 KNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQAlskrvvpRLRALIVVPTKELVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 71 QVASHIRDIGRYMDTKVAEVYGGMPYKAQINRVR---------NADIVVATPGRLLD-LWSKGVIDLSSFEIVIIDEAD- 139
Cdd:cd17956 83 QVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLvdtsgrylsRVDILVATPGRLVDhLNSTPGFTLKHLRFLVIDEADr 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
2Z0M_A 140 ------------LMFEMG---------FIDDIKIILAQTSNRKItgLFSATI---PEEI 174
Cdd:cd17956 163 llnqsfqdwletVMKALGrptapdlgsFGDANLLERSVRPLQKL--LFSATLtrdPEKL 219
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
1-184 |
1.98e-25 |
|
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: 101.00 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPIL---ELGMKS---LVVTPTRELTRQVAS 74
Cdd:cd18045 6 LREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLqclDIQVREtqaLILSPTRELAVQIQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 75 HIRDIGRYMDTKVAEVYGGMPYKAQINRVRNA-DIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKII 153
Cdd:cd18045 86 VLLALGDYMNVQCHACIGGTSVGDDIRKLDYGqHIVSGTPGRVFDMIRRRSLRTRHIKMLVLDEADEMLNKGFKEQIYDV 165
|
170 180 190
....*....|....*....|....*....|.
2Z0M_A 154 LAQTSNRKITGLFSATIPEEIRKVVKDFITN 184
Cdd:cd18045 166 YRYLPPATQVVLVSATLPQDILEMTNKFMTD 196
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
235-311 |
8.46e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 87.65 E-value: 8.46e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2Z0M_A 235 KLVRLFDNAIELRGDLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKVINFDAPQDLRTYIHRIGRTGRMG 311
Cdd:smart00490 6 LLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
3-317 |
2.98e-20 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 91.50 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 3 EKIEQAIREMGFKNFTEVQSKTIP-LMLQGKNVVVRAKTGSGKTAAYAIPI---LELGMKSLVVTPTRELTRQVASHIRD 78
Cdd:COG1204 9 EKVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAIlkaLLNGGKALYIVPLRALASEKYREFKR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 79 IGRYMDTKVAEVYGgmPYKAQINRVRNADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLmfemgfIDD--------- 149
Cdd:COG1204 89 DFEELGIKVGVSTG--DYDSDDEWLGRYDILVATPEKLDSLLRNGPSWLRDVDLVVVDEAHL------IDDesrgptlev 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 150 -IKIILAQTSNRKITGLfSATIPeeirkvvkdfitNYEEIEACIGLANVE--------HKFVHVKDD--WRSKVQALRE- 217
Cdd:COG1204 161 lLARLRRLNPEAQIVAL-SATIG------------NAEEIAEWLDAELVKsdwrpvplNEGVLYDGVlrFDDGSRRSKDp 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 218 ---------NKDKGVIVFVRTRN-------RVAKLVRLFDN----------AIELR------------------------ 247
Cdd:COG1204 228 tlalaldllEEGGQVLVFVSSRRdaeslakKLADELKRRLTpeereeleelAEELLevseethtnekladclekgvafhh 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2Z0M_A 248 GDLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPlVEKVI------NFDAPQDLRTYIHRIGRTGRMGR--KGEAI 317
Cdd:COG1204 308 AGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIirdtkrGGMVPIPVLEFKQMAGRAGRPGYdpYGEAI 384
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
31-169 |
4.85e-19 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 82.45 E-value: 4.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 31 GKNVVVRAKTGSGKTAAYAIPILEL----GMKSLVVTPTRELTRQVASHIRDIGRyMDTKVAEVYGGMPYKAQ-INRVRN 105
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLllkkGKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEReKNKLGD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
2Z0M_A 106 ADIVVATPGRLL-DLWSKGVIDLSSFEIVIIDEADLM---FEMGFIDDIKIILAQTSNRKITGLfSAT 169
Cdd:cd00046 80 ADIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALlidSRGALILDLAVRKAGLKNAQVILL-SAT 146
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
31-320 |
9.09e-19 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 87.00 E-value: 9.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 31 GKNVVVRAKTGSGKT--AAYAIPILELGMKSLVVTPTRELTRQVASHIRDIgrymdTKVAEVYGGmpykaqiNRVRNADI 108
Cdd:COG1061 100 GGRGLVVAPTGTGKTvlALALAAELLRGKRVLVLVPRRELLEQWAEELRRF-----LGDPLAGGG-------KKDSDAPI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 109 VVATPGrllDLWSKGVIDL--SSFEIVIIDEADLMFEMGFIDdikiILAQTSNRKITGLfSATiPEeiRKVVKD-FITNY 185
Cdd:COG1061 168 TVATYQ---SLARRAHLDElgDRFGLVIIDEAHHAGAPSYRR----ILEAFPAAYRLGL-TAT-PF--RSDGREiLLFLF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 186 EEIEACIGLAN-------VEHKFVHVKDDWRS----------------------KVQALRE-----NKDKGVIVFVRTRN 231
Cdd:COG1061 237 DGIVYEYSLKEaiedgylAPPEYYGIRVDLTDeraeydalserlrealaadaerKDKILREllrehPDDRKTLVFCSSVD 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 232 RVAKLVRLFD----NAIELRGDLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKVINFDAPQDLRTYIHRIGRT 307
Cdd:COG1061 317 HAEALAELLNeagiRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRG 396
|
330
....*....|...
2Z0M_A 308 GRMGRKGEAITFI 320
Cdd:COG1061 397 LRPAPGKEDALVY 409
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
1-330 |
2.72e-16 |
|
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: 79.88 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREMGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILEL-----GMKSLVVTPTRELTR-QVAS 74
Cdd:COG1205 41 LPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAlledpGATALYLYPTKALARdQLRR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 75 hIRDIGRYMDTKV-AEVY-GGMPyKAQINRVR-NADIVVATPgrllDLWSKGVID--------LSSFEIVIIDEA----- 138
Cdd:COG1205 121 -LRELAEALGLGVrVATYdGDTP-PEERRWIReHPDIVLTNP----DMLHYGLLPhhtrwarfFRNLRYVVIDEAhtyrg 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 139 --------------DLMFEMGfiDDIKIILAqtsnrkitglfSATI--PEEIrkvvkdfitnyeeIEACIGLanvehKFV 202
Cdd:COG1205 195 vfgshvanvlrrlrRICRHYG--SDPQFILA-----------SATIgnPAEH-------------AERLTGR-----PVT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 203 HVKDD-----------W----------RSKVQA----LRENKDKGV--IVFVRTRNRVAKLVRLFDNAIEL--------- 246
Cdd:COG1205 244 VVDEDgsprgertfvlWnpplvddgirRSALAEaarlLADLVREGLrtLVFTRSRRGAELLARYARRALREpdladrvaa 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 247 -RGDLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKVINFDAPQDLRTYIHRIGRTGRMGRKGEAI-------- 317
Cdd:COG1205 324 yRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVlvagddpl 403
|
410
....*....|....*.
2Z0M_A 318 -TFILN--EYWLEKEV 330
Cdd:COG1205 404 dQYYVRhpEELFERPP 419
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
1-174 |
2.99e-16 |
|
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated testicular RNA helicase (GRTH) is a testis-specific protein essential for completion of spermatogenesis. DDX25 is also a novel negative regulator of IFN pathway and facilitates RNA virus infection. Diseases associated with DDX25 include hydrolethalus syndrome, an autosomal recessive lethal malformation syndrome characterized by multiple developmental defects of fetus.. DDX25 (also called gonadotropin-regulated testicular RNA helicase) is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350806 [Multi-domain] Cd Length: 229 Bit Score: 76.60 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREMGFKNFTEVQSKTIPLMLQG--KNVVVRAKTGSGKTAAYAIPIL------ELGMKSLVVTPTRELTRQV 72
Cdd:cd18048 25 LKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLsrvdalKLYPQCLCLSPTFELALQT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 73 ASHIRDIGRY-MDTKVA-EVYGGMPYK-AQInrvrNADIVVATPGRLLDLWSK-GVIDLSSFEIVIIDEADLMFEM-GFI 147
Cdd:cd18048 105 GKVVEEMGKFcVGIQVIyAIRGNRPGKgTDI----EAQIVIGTPGTVLDWCFKlRLIDVTNISVFVLDEADVMINVqGHS 180
|
170 180
....*....|....*....|....*...
2Z0M_A 148 D-DIKIILAQTSNRKITgLFSATIPEEI 174
Cdd:cd18048 181 DhSVRVKRSMPKECQML-LFSATFEDSV 207
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
18-181 |
1.03e-15 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 75.49 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 18 TEVQSKTIPLMLQG----------------KNVVVRAKTGSGKTAAYAIPILEL-----------------------GMK 58
Cdd:cd17965 32 SPIQTLAIKKLLKTlmrkvtkqtsneepklEVFLLAAETGSGKTLAYLAPLLDYlkrqeqepfeeaeeeyesakdtgRPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 59 SLVVTPTRELTRQVASHIRDIGRYMDTKVAEVYGGM--PYKAQINRVRNA-DIVVATPGRLLDLWSKGVIDLSSFEIVII 135
Cdd:cd17965 112 SVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFgpSYQRLQLAFKGRiDILVTTPGKLASLAKSRPKILSRVTHLVV 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
2Z0M_A 136 DEADLMFEMGFIDDIKIILAQTSNRKITGLFSATIPEEIRKVVKDF 181
Cdd:cd17965 192 DEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLRKL 237
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
17-171 |
3.11e-15 |
|
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: 72.68 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 17 FTEVQSKTI-PLMLQGKNVVVRAKTGSGKT--AAYAI--PILELGMKSLVVTPTRELTRQVASHIRDIGRYMDTKVAEVY 91
Cdd:cd17921 2 LNPIQREALrALYLSGDSVLVSAPTSSGKTliAELAIlrALATSGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGLLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 92 GGmpYKAQINRVRNADIVVATPGRLLDLWSKGVID-LSSFEIVIIDEADLMF--EMGFI--DDIKIILAQTSNRKITGLf 166
Cdd:cd17921 82 GD--PSVNKLLLAEADILVATPEKLDLLLRNGGERlIQDVRLVVVDEAHLIGdgERGVVleLLLSRLLRINKNARFVGL- 158
|
....*
2Z0M_A 167 SATIP 171
Cdd:cd17921 159 SATLP 163
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
1-176 |
1.14e-13 |
|
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: 68.98 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREMGFKNFTEVQSKTIPLMLQG--KNVVVRAKTGSGKTAAYAIPILE------LGMKSLVVTPTRELTRQV 72
Cdd:cd18047 8 LKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSqvepanKYPQCLCLSPTYELALQT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 73 ASHIRDIGR-YMDTKVAEVYGGMPYKAQInRVRNaDIVVATPGRLLDLWSK-GVIDLSSFEIVIIDEADLMFEMGFIDDI 150
Cdd:cd18047 88 GKVIEQMGKfYPELKLAYAVRGNKLERGQ-KISE-QIVIGTPGTVLDWCSKlKFIDPKKIKVFVLDEADVMIATQGHQDQ 165
|
170 180
....*....|....*....|....*..
2Z0M_A 151 KIILAQTSNRKITG-LFSATIPEEIRK 176
Cdd:cd18047 166 SIRIQRMLPRNCQMlLFSATFEDSVWK 192
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
213-322 |
7.71e-13 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 69.37 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 213 QALRENKDKGVIVFVRTRNRVAKLV-RLFDNAIELRGDLPQSVRNRN-----------IDAFREGEYDMLITTDVASRGL 280
Cdd:COG1111 346 EQLGTNPDSRIIVFTQYRDTAEMIVeFLSEPGIKAGRFVGQASKEGDkgltqkeqieiLERFRAGEFNVLVATSVAEEGL 425
|
90 100 110 120
....*....|....*....|....*....|....*....|...
2Z0M_A 281 DIPLVEKVINFDA-PQDLRtYIHRIGRTGRmGRKGEAITFILN 322
Cdd:COG1111 426 DIPEVDLVIFYEPvPSEIR-SIQRKGRTGR-KREGRVVVLIAK 466
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
210-310 |
2.89e-12 |
|
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: 63.38 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 210 SKVQALRE--------NKDKGVIVFVRTRNRVAKLVRLFDNAIELRGDL-PQSVRNRN------------------IDAF 262
Cdd:cd18802 7 PKLQKLIEilreyfpkTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIrCGFLIGRGnssqrkrslmtqrkqketLDKF 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
2Z0M_A 263 REGEYDMLITTDVASRGLDIPLVEKVINFDAPQDLRTYIHRIGRtGRM 310
Cdd:cd18802 87 RDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
215-317 |
5.74e-12 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 66.82 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 215 LRENKDKGVIVFVRTRNRVAKLV-RLFDNAIELRGDLPQSVRNRN-----------IDAFREGEYDMLITTDVASRGLDI 282
Cdd:PRK13766 360 LGKNPDSRIIVFTQYRDTAEKIVdLLEKEGIKAVRFVGQASKDGDkgmsqkeqieiLDKFRAGEFNVLVSTSVAEEGLDI 439
|
90 100 110
....*....|....*....|....*....|....*.
2Z0M_A 283 PLVEKVINFDA-PQDLRTyIHRIGRTGRmGRKGEAI 317
Cdd:PRK13766 440 PSVDLVIFYEPvPSEIRS-IQRKGRTGR-QEEGRVV 473
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
200-314 |
6.71e-12 |
|
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: 62.37 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 200 KFVHVKDDWRSKVQALRENKDKGVIVFVRTRNRVAKLVRLFD---------------NAIELRGdLPQSVRNRNIDAFRE 264
Cdd:cd18801 10 KLEKLEEIVKEHFKKKQEGSDTRVIIFSEFRDSAEEIVNFLSkirpgiratrfigqaSGKSSKG-MSQKEQKEVIEQFRK 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
2Z0M_A 265 GEYDMLITTDVASRGLDIPLVEKVINFDA-PQDLRTyIHRIGRTGRmGRKG 314
Cdd:cd18801 89 GGYNVLVATSIGEEGLDIGEVDLIICYDAsPSPIRM-IQRMGRTGR-KRQG 137
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
32-138 |
4.24e-11 |
|
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: 61.51 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 32 KNVVVRAKTGSGKTAAYAIPILEL----------GMKSLVVTPTRELTRQVASHIRdigRYMDTKVAEVYGGMPYKAQI- 100
Cdd:cd18034 17 RNTIVVLPTGSGKTLIAVMLIKEMgelnrkeknpKKRAVFLVPTVPLVAQQAEAIR---SHTDLKVGEYSGEMGVDKWTk 93
|
90 100 110 120
....*....|....*....|....*....|....*....|..
2Z0M_A 101 ----NRVRNADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEA 138
Cdd:cd18034 94 erwkEELEKYDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
21-138 |
1.14e-10 |
|
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: 59.91 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 21 QSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILEL-----GMKSLVVTPTRELTRQVASHIRDIGRYMDTKV-AEVYGG- 93
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAllrdpGSRALYLYPTKALAQDQLRSLRELLEQLGLGIrVATYDGd 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
2Z0M_A 94 MPYKAQINRVRN-ADIVVATPGRL-------LDLWSKgviDLSSFEIVIIDEA 138
Cdd:cd17923 85 TPREERRAIIRNpPRILLTNPDMLhyallphHDRWAR---FLRNLRYVVLDEA 134
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
28-309 |
5.76e-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: 57.19 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 28 MLQGKNVVVRAKTGSGKT------AAYAipiLELGMKSLVVTPTRELTRQVASHIRDIgrYMDTKVAEVYGGMPykaqiN 101
Cdd:COG4098 126 IKKKEEHLVWAVCGAGKTemlfpaIAEA---LKQGGRVCIATPRVDVVLELAPRLQQA--FPGVDIAALYGGSE-----E 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 102 RVRNADIVVATPGRLLDLWSkgvidlsSFEIVIIDEADlMFEmgFIDDikIILAQTSN--RKITG---LFSATIPEEIRK 176
Cdd:COG4098 196 KYRYAQLVIATTHQLLRFYQ-------AFDLLIIDEVD-AFP--YSGD--PMLQYAVKraRKPDGkliYLTATPSKALQR 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 177 VVKdfitnyEEIEACIGLANVEH-------KFVHVKdDWRSKVQ------------ALRENKDKGVIVFVRTRNRVAKLV 237
Cdd:COG4098 264 QVK------RGKLKVVKLPARYHghplpvpKFKWLG-NWKKRLRrgklprkllkwlKKRLKEGRQLLIFVPTIELLEQLV 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 238 RLFDNaiELRGDLPQSV------RNRNIDAFREGEYDMLITTDVASRGLDIPLVEkVINFDAPqdlrtyiHRI------- 304
Cdd:COG4098 337 ALLQK--LFPEERIAGVhaedpeRKEKVQAFRDGEIPILVTTTILERGVTFPNVD-VAVLGAD-------HPVfteaalv 406
|
....*...
2Z0M_A 305 ---GRTGR 309
Cdd:COG4098 407 qiaGRVGR 414
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
16-137 |
9.68e-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: 54.67 E-value: 9.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 16 NFTEVQSKTIPLMLQG-KNVVVRAKTGSGKTAAYAIPILELGMKSLVVT----------PTRELTRQVASHIRDIGRYMD 84
Cdd:cd18023 1 YFNRIQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERNPLPwgnrkvvyiaPIKALCSEKYDDWKEKFGPLG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
2Z0M_A 85 TKVAEVYGGMPYKaQINRVRNADIVVATPGR---LLDLWSKGVIDLSSFEIVIIDE 137
Cdd:cd18023 81 LSCAELTGDTEMD-DTFEIQDADIILTTPEKwdsMTRRWRDNGNLVQLVALVLIDE 135
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
34-321 |
1.07e-08 |
|
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: 55.90 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 34 VVVRAKTGSGKT---AAYAIPILELGM--KSLVVTPTRELT-------RQVASHIRDIGRYMDTKVAEVYGGMPYKAQI- 100
Cdd:cd09639 2 LVIEAPTGYGKTeaaLLWALHSLKSQKadRVIIALPTRATInamyrraKEAFGETGLYHSSILSSRIKEMGDSEEFEHLf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 101 -------NRVRNADIVVATPGRLLDLWSKGV--IDLSSFEI----VIIDEADLM--FEMGFIddIKIILAQTSNRKITGL 165
Cdd:cd09639 82 plyihsnDTLFLDPITVCTIDQVLKSVFGEFghYEFTLASIanslLIFDEVHFYdeYTLALI--LAVLEVLKDNDVPILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 166 FSATIPEEIRKVVKDfITNYEEIEACIGLANVEHKFVHVKDDWRSKVQALRE-----NKDKGVIVFVRTRNR-VAKLVRL 239
Cdd:cd09639 160 MSATLPKFLKEYAEK-IGYVEENEPLDLKPNERAPFIKIESDKVGEISSLERllefiKKGGSVAIIVNTVDRaQEFYQQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 240 FDNAIELRGDLPQS---------VRNRNIDAFREGEYDMLITTDVASRGLDIPlVEKVINFDAPQDLrtYIHRIGRTGRM 310
Cdd:cd09639 239 KEKGPEEEIMLIHSrftekdrakKEAELLLEFKKSEKFVIVATQVIEASLDIS-VDVMITELAPIDS--LIQRLGRLHRY 315
|
330
....*....|.
2Z0M_A 311 GRKGEAITFIL 321
Cdd:cd09639 316 GEKNGEEVYII 326
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
29-139 |
3.05e-08 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 53.10 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 29 LQGKNVVVRAKTGSGKT---AAYAIPILELGMKSLVVTPTRELTRQVASHIRDIGRYMDTKVAEVY--GGMPYKAQIN-- 101
Cdd:cd17924 30 LRGKSFAIIAPTGVGKTtfgLATSLYLASKGKRSYLIFPTKSLVKQAYERLSKYAEKAGVEVKILVyhSRLKKKEKEEll 109
|
90 100 110 120
....*....|....*....|....*....|....*....|...
2Z0M_A 102 ---RVRNADIVVATPGRLldlwSKGVIDLSS--FEIVIIDEAD 139
Cdd:cd17924 110 ekiEKGDFDILVTTNQFL----SKNFDLLSNkkFDFVFVDDVD 148
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
6-319 |
1.14e-07 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 53.18 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 6 EQAIRE-MGFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILELGMKSLVVTPTRELTRQVASHIRDIGrymd 84
Cdd:PRK11057 14 KQVLQEtFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANG---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 85 TKVAEVYGGMPYKAQ---INRVRNADI--VVATPGRLLdlwSKGVID-LSSFEIVII--DEA--------DLMFEMGFID 148
Cdd:PRK11057 90 VAAACLNSTQTREQQlevMAGCRTGQIklLYIAPERLM---MDNFLEhLAHWNPALLavDEAhcisqwghDFRPEYAALG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 149 DIKiilAQTSNRKITGLfSATIPEEIRKvvkDFITNYEEIEACIGLAN----------VEhKFVHVKDDWRSkvqaLREN 218
Cdd:PRK11057 167 QLR---QRFPTLPFMAL-TATADDTTRQ---DIVRLLGLNDPLIQISSfdrpnirytlVE-KFKPLDQLMRY----VQEQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 219 KDKGVIVFVRTRNRVAKLV-RLFDNAIELRG---DLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKVINFDAP 294
Cdd:PRK11057 235 RGKSGIIYCNSRAKVEDTAaRLQSRGISAAAyhaGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIP 314
|
330 340
....*....|....*....|....*
2Z0M_A 295 QDLRTYIHRIGRTGRMGRKGEAITF 319
Cdd:PRK11057 315 RNIESYYQETGRAGRDGLPAEAMLF 339
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
1-317 |
1.64e-07 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 52.90 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREMGFKNFTEVQSKTIPL-MLQGKNVVVRAKTGSGKTAAYAI----PILELGMKSLVVTPTRELTRQVASH 75
Cdd:PRK00254 8 VDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIvmvnKLLREGGKAVYLVPLKALAEEKYRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 76 IRDIGRyMDTKVAEVYGGmpYKAQINRVRNADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEMGFIDDIKIILA 155
Cdd:PRK00254 88 FKDWEK-LGLRVAMTTGD--YDSTDEWLGKYDIIIATAEKFDSLLRHGSSWIKDVKLVVADEIHLIGSYDRGATLEMILT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 156 QTSNR-KITGLfSATI--PEEIRKVV--KDFITNYEEIEACIGLanVEHKFVHVKD--------DWRSKV-QALRenKDK 221
Cdd:PRK00254 165 HMLGRaQILGL-SATVgnAEELAEWLnaELVVSDWRPVKLRKGV--FYQGFLFWEDgkierfpnSWESLVyDAVK--KGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 222 GVIVFVRTRNR-------VAKLVRLFDNAIELRG---------------DLPQSVRN-------------RNI--DAFRE 264
Cdd:PRK00254 240 GALVFVNTRRSaekealeLAKKIKRFLTKPELRAlkeladsleenptneKLKKALRGgvafhhaglgrteRVLieDAFRE 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
2Z0M_A 265 GEYDMLITTDVASRGLDIPLVEKVInfdapQDLRTY------------IHR-IGRTGR--MGRKGEAI 317
Cdd:PRK00254 320 GLIKVITATPTLSAGINLPAFRVII-----RDTKRYsnfgwedipvleIQQmMGRAGRpkYDEVGEAI 382
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
270-320 |
2.41e-07 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 47.70 E-value: 2.41e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
2Z0M_A 270 LITTDVASRGLDIPLVEKVINFDAPQDLRTYIHRIGRTGR-MGRKGEAITFI 320
Cdd:cd18785 26 LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRgGKDEGEVILFV 77
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
28-200 |
6.79e-07 |
|
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: 48.87 E-value: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 28 MLQGKNVVVRAKTGSGKT--AAYAI--PILElGMKSLVVTPTRELTRQVASHIRDIGRyMDTKVAeVYGGMpYKAQINRV 103
Cdd:cd18028 14 LLKGENLLISIPTASGKTliAEMAMvnTLLE-GGKALYLVPLRALASEKYEEFKKLEE-IGLKVG-ISTGD-YDEDDEWL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 104 RNADIVVATPGRLLDLWSKGVIDLSSFEIVIIDEADLMFEM--GFIDDIKIILAQTSN--RKITGLfSATIPeeirkvvk 179
Cdd:cd18028 90 GDYDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEerGPTLESIVARLRRLNpnTQIIGL-SATIG-------- 160
|
170 180
....*....|....*....|.
2Z0M_A 180 dfitNYEEIEACIGLANVEHK 200
Cdd:cd18028 161 ----NPDELAEWLNAELVESD 177
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
1-319 |
1.36e-06 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 49.75 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 1 MNEKIEQAIREM-GFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILELGMKSLVVTPTRELTR-QVAShIRD 78
Cdd:COG0514 1 LRDDALEVLKRVfGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKdQVDA-LRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 79 IGrymdTKVAEVYGGMPYkAQINRVRNA------DIVVATPGRLLdlwSKGVID-LSSFEI--VIIDEA--------Dlm 141
Cdd:COG0514 80 AG----IRAAFLNSSLSA-EERREVLRAlragelKLLYVAPERLL---NPRFLElLRRLKIslFAIDEAhcisqwghD-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 142 femgFIDD---IKIILAQTSNRKITGLfSATIPEEIRkvvkdfitnyEEIEACIGLAN----------------VEHKFV 202
Cdd:COG0514 150 ----FRPDyrrLGELRERLPNVPVLAL-TATATPRVR----------ADIAEQLGLEDprvfvgsfdrpnlrleVVPKPP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 203 HVKDDWRskVQALRENKDKGVIVFVRTRNRVAKLvrlfdnAIELR----------GDLPQSVRNRNIDAFREGEYDMLIT 272
Cdd:COG0514 215 DDKLAQL--LDFLKEHPGGSGIVYCLSRKKVEEL------AEWLReagiraaayhAGLDAEEREANQDRFLRDEVDVIVA 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
2Z0M_A 273 TdVA-SRGLDIPLVEKVINFDAPQDLRTYIHRIGRTGRMGRKGEAITF 319
Cdd:COG0514 287 T-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLL 333
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
29-138 |
1.49e-06 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 48.20 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 29 LQGKNVVVRAKTGSGKTAA---------YAIPILELGmKSLVVTPTRELTRQVASHIRDIGRYMDTKVAEVYGGMPYKAQ 99
Cdd:cd17927 15 LKGKNTIICLPTGSGKTFVavlicehhlKKFPAGRKG-KVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLSGDTSENVS 93
|
90 100 110 120
....*....|....*....|....*....|....*....|.
2Z0M_A 100 INRV-RNADIVVATPGRLL-DLWSKGVIDLSSFEIVIIDEA 138
Cdd:cd17927 94 VEQIvESSDVIIVTPQILVnDLKSGTIVSLSDFSLLVFDEC 134
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
14-317 |
2.22e-06 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 49.33 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 14 FKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKT-AAYAIPILEL-----------GMKSLVVTPTRELTrqvashiRDIGR 81
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPALDELarrprpgelpdGLRVLYISPLKALA-------NDIER 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 82 YMDTKVAEVYGGMPYKAQINRV-----------RNA------DIVVATPGRL-LDLWSKGVID-LSSFEIVIIDE----- 137
Cdd:COG1201 95 NLRAPLEEIGEAAGLPLPEIRVgvrtgdtpaseRQRqrrrppHILITTPESLaLLLTSPDARElLRGVRTVIVDEihala 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 138 -----ADLMFEMGFIDDikiiLAQTSNRKItGLfSATI--PEEIRKV-----------------VKDFitnyeEIEACIG 193
Cdd:COG1201 175 gskrgVHLALSLERLRA----LAPRPLQRI-GL-SATVgpLEEVARFlvgyedprpvtivdagaGKKP-----DLEVLVP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 194 LANVEHKFVHVKDDWRSKVQALRE--NKDKGVIVFVRTRnRVAKlvRLFDNAIELRGDLP-----------QSVRNRNID 260
Cdd:COG1201 244 VEDLIERFPWAGHLWPHLYPRVLDliEAHRTTLVFTNTR-SQAE--RLFQRLNELNPEDAlpiaahhgslsREQRLEVEE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 261 AFREGEYDMLITTdvAS--RGLDIPLVEKVINFDAPQDLRTYIHRIGRTG-RMGRKGEAI 317
Cdd:COG1201 321 ALKAGELRAVVAT--SSleLGIDIGDVDLVIQVGSPKSVARLLQRIGRAGhRVGEVSKGR 378
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
199-319 |
3.01e-06 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 46.05 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 199 HKFVHVKDDWRSKVQALRE----NKDKGVIVFVRTRN---RVAK-LVRLFDNAIELRGDLPQSVRNRNIDAFREGEYDML 270
Cdd:cd18794 5 FYSVRPKDKKDEKLDLLKRikveHLGGSGIIYCLSRKeceQVAArLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVI 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
2Z0M_A 271 ITTDVASRGLDIPLVEKVINFDAPQDLRTYIHRIGRTGRMGRKGEAITF 319
Cdd:cd18794 85 VATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILF 133
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
212-305 |
3.17e-06 |
|
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: 45.93 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 212 VQALRENKDKgVIVF---VRTRNRVAK-LVRLFDNAIELRGDLPQSVRNRNIDAFREGEYD--MLITTDVASRGLDIPLV 285
Cdd:cd18793 20 LEELREPGEK-VLIFsqfTDTLDILEEaLRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNLTAA 98
|
90 100
....*....|....*....|....*...
2Z0M_A 286 EKVINFDA---PQDL-----RtyIHRIG 305
Cdd:cd18793 99 NRVILYDPwwnPAVEeqaidR--AHRIG 124
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
196-310 |
4.96e-06 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350185 [Multi-domain] Cd Length: 174 Bit Score: 46.14 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 196 NVEHKFVHVKDDWRSKVQALRENKDkGVIVFVRTRNRVAKLVRLFDNAIE--LRGDLPQSVRNRNIDAFREGEYDMLITT 273
Cdd:cd18798 1 NIVDVYIEDSDSLEKLLELVKKLGD-GGLIFVSIDYGKEYAEELKEFLERhgIKAELALSSTEKNLEKFEEGEIDVLIGV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
2Z0M_A 274 ----DVASRGLDIPLVEK-VINFDAPqdLRTYIHRIGRTGRM 310
Cdd:cd18798 80 asyyGVLVRGIDLPERIKyAIFYGVP--VTTYIQASGRTSRL 119
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
219-321 |
7.05e-06 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 45.33 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 219 KDKGVIVFVRTRNRVAKLVRLFDNAIELRGD----------LPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKV 288
Cdd:cd18796 37 RHKSTLVFTNTRSQAERLAQRLRELCPDRVPpdfialhhgsLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLV 116
|
90 100 110
....*....|....*....|....*....|...
2Z0M_A 289 INFDAPQDLRTYIHRIGRTGRmgRKGEAITFIL 321
Cdd:cd18796 117 IQIGSPKSVARLLQRLGRSGH--RPGAASKGRL 147
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
209-316 |
2.42e-05 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 43.78 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 209 RSKVQALR------ENKDKgVIVFVRTrnrVAKLVRLfdnAIELR-----GDLPQSVRNRNIDAFREGEYDMLITTDVAS 277
Cdd:cd18789 33 PNKLRALEellkrhEQGDK-IIVFTDN---VEALYRY---AKRLLkpfitGETPQSEREEILQNFREGEYNTLVVSKVGD 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
2Z0M_A 278 RGLDIPlvekvinfDA---------PQDLRTYIHRIGRTGRMGRKGEA 316
Cdd:cd18789 106 EGIDLP--------EAnvaiqisghGGSRRQEAQRLGRILRPKKGGGK 145
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
14-55 |
3.35e-05 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 45.65 E-value: 3.35e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
2Z0M_A 14 FKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKT-AAYAIPILEL 55
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFLAIIDEL 72
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
6-138 |
4.01e-05 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 44.06 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 6 EQAIREM-GFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILELGMKSLVVTPTRELTR-QVaSHIRDIGRym 83
Cdd:cd17920 1 EQILKEVfGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQdQV-DRLQQLGI-- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2Z0M_A 84 dtKVAEVYGGMPY---KAQINRVRN--ADIVVATPGRLLD---------LWSKGVIDLssfeiVIIDEA 138
Cdd:cd17920 78 --RAAALNSTLSPeekREVLLRIKNgqYKLLYVTPERLLSpdflellqrLPERKRLAL-----IVVDEA 139
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
33-137 |
5.09e-05 |
|
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: 43.17 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 33 NVVVRAKTGSGKTAAYAIPIL---ELGMKSLVVTPTRELTRQVASHIRDigRYMDTKVAEVYGGmpYKAQINrvRNADIV 109
Cdd:cd17918 38 DRLLSGDVGSGKTLVALGAALlayKNGKQVAILVPTEILAHQHYEEARK--FLPFINVELVTGG--TKAQIL--SGISLL 111
|
90 100
....*....|....*....|....*...
2Z0M_A 110 VATPGrLLDLWSKGvidlSSFEIVIIDE 137
Cdd:cd17918 112 VGTHA-LLHLDVKF----KNLDLVIVDE 134
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
29-137 |
7.00e-05 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350831 [Multi-domain] Cd Length: 202 Bit Score: 43.27 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 29 LQGKNVVVRAKTGSGKTAAyAIPILE-------LGMKSLVV-----TPTRELTRQVASHIRDIGRYmdtKVAEVYGGMPY 96
Cdd:cd18073 15 MKGKNTIICAPTGCGKTFV-SLLICEhhlkkfpQGQKGKVVffatkVPVYEQQKSVFSKYFERHGY---RVTGISGATAE 90
|
90 100 110 120
....*....|....*....|....*....|....*....|...
2Z0M_A 97 KAQINRV-RNADIVVATPGRLLDLWSKGVI-DLSSFEIVIIDE 137
Cdd:cd18073 91 NVPVEQIiENNDIIILTPQILVNNLKKGTIpSLSIFTLMIFDE 133
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
32-113 |
9.16e-05 |
|
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350780 [Multi-domain] Cd Length: 189 Bit Score: 42.75 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 32 KNVVVRAKTGSGKTAAYAIPILEL-----GMKSLVVTPTRELTRQ-VASHIRDIGRYMDTKVAEVYGGmpYKAQINRVRN 105
Cdd:cd18022 18 NNVLLGAPTGSGKTIAAELAMFRAfnkypGSKVVYIAPLKALVRErVDDWKKRFEEKLGKKVVELTGD--VTPDMKALAD 95
|
....*...
2Z0M_A 106 ADIVVATP 113
Cdd:cd18022 96 ADIIITTP 103
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
206-317 |
1.02e-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: 41.86 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 206 DDWRSKVQALRENK-------DKGV--IVFVRTRNRVAKLVRLFDNAIE-----------LRGDLPQSVRNRNIDAFREG 265
Cdd:cd18797 12 RKDGERGSARREAArlfadlvRAGVktIVFCRSRKLAELLLRYLKARLVeegplaskvasYRAGYLAEDRREIEAELFNG 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
2Z0M_A 266 EYDMLITTDVASRGLDIPLVEKVINFDAPQDLRTYIHRIGRTGRMGRKGEAI 317
Cdd:cd18797 92 ELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| DEXDc_ComFA |
cd17925 |
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon ... |
30-139 |
1.37e-04 |
|
DEXD-box helicase domain of ComFA; ATP-dependent helicase ComFA (also called ComF operon protein 1) is part of the complex mediating the binding and uptake of single-stranded DNA. ComFA is required for DNA uptake but not for binding. It 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: 350683 [Multi-domain] Cd Length: 143 Bit Score: 41.52 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 30 QGKNVVVRAKTGSGKT-AAYAI--PILELGMKSLVVTPTRELTRQVASHIRDIGRYMDtkVAEVYGGMPYKAQinrvrNA 106
Cdd:cd17925 15 AKEDLLVWAVTGAGKTeMLFPAiaQALRQGGRVAIASPRIDVCLELAPRLKAAFPGAA--IVLLHGGSEDQYQ-----RS 87
|
90 100 110
....*....|....*....|....*....|...
2Z0M_A 107 DIVVATPGRLLDLWskgvidlSSFEIVIIDEAD 139
Cdd:cd17925 88 PLVIATTHQLLRFY-------RAFDLLIIDEVD 113
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
224-306 |
2.63e-04 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 39.85 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 224 IVFVRTRNRVAKLVRLFDNA----IELRGDLPQSVRNRNI---DAFREGEYDMLITTDVASRGLDIPLVEKVInFDAPQD 296
Cdd:cd18799 10 LIFCVSIEHAEFMAEAFNEAgidaVALNSDYSDRERGDEAlilLFFGELKPPILVTVDLLTTGVDIPEVDNVV-FLRPTE 88
|
90
....*....|.
2Z0M_A 297 LRT-YIHRIGR 306
Cdd:cd18799 89 SRTlFLQMLGR 99
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
232-317 |
5.82e-04 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 40.69 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 232 RVAKLVR-LFDNAIELRGDLpQSVRNRN-----IDAFREGEYDMLITTDVASRGLDIPLVEKVINFDAPQDL-------- 297
Cdd:cd18804 105 RVEEELKtLFPEARIARIDR-DTTRKKGaleklLDQFERGEIDILIGTQMIAKGLDFPNVTLVGILNADSGLnspdfras 183
|
90 100
....*....|....*....|....
2Z0M_A 298 -RTY--IHRI-GRTGRMGRKGEAI 317
Cdd:cd18804 184 eRAFqlLTQVsGRAGRGDKPGKVI 207
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
31-137 |
7.09e-04 |
|
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: 39.87 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 31 GKNVVVRAKTGSGKTAAYAIPIL-------ELGMKSLVVTPTRELtrqvashIRDIGRYMDTKVAEVYGGMPY------- 96
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALssladepEKGVQVLYISPLKAL-------INDQERRLEEPLDEIDLEIPVavrhgdt 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
2Z0M_A 97 ----KAQInRVRNADIVVATPGRL-LDLWSKGVI-DLSSFEIVIIDE 137
Cdd:cd17922 74 sqseKAKQ-LKNPPGILITTPESLeLLLVNKKLReLFAGLRYVVVDE 119
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
6-138 |
1.00e-03 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 39.55 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 6 EQAIREM-GFKNFTEVQSKTIPLMLQGKNVVVRAKTGSGKTAAYAIPILELGMKS----LVVTPTRELTR-QVASHIRDI 79
Cdd:cd18018 1 LKLLRRVfGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGpgltLVVSPLIALMKdQVDALPRAI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 80 grymdtKVAEVYGGMP---YKAQINRVRNA--DIVVATPGRLLD------LWSKGVIDLssfeiVIIDEA 138
Cdd:cd18018 81 ------KAAALNSSLTreeRRRILEKLRAGevKILYVSPERLVNesfrelLRQTPPISL-----LVVDEA 139
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
32-138 |
1.53e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 38.81 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 32 KNVVVRAKTGSGKTAAYAIPILEL-----GMKSLVVTPTRELTRQVASHIRDIGrYMDTKVAEVYGGmpyKAQINRVRNA 106
Cdd:pfam04851 24 KRGLIVMATGSGKTLTAAKLIARLfkkgpIKKVLFLVPRKDLLEQALEEFKKFL-PNYVEIGEIISG---DKKDESVDDN 99
|
90 100 110
....*....|....*....|....*....|....*
2Z0M_A 107 DIVVATP---GRLLDLWSKGVIDlSSFEIVIIDEA 138
Cdd:pfam04851 100 KIVVTTIqslYKALELASLELLP-DFFDVIIIDEA 133
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
3-171 |
2.10e-03 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 38.74 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 3 EKIEQAIREMGFKNFTEVQSK--TIPLMLQGKNVVVRAKTGSGKTAAYAIPIL----ELGMKSLVVTPTRELTRQVASHI 76
Cdd:cd18026 3 DAVREAYAKKGIKKLYDWQKEclSLPGLLEGRNLVYSLPTSGGKTLVAEILMLkrllERRKKALFVLPYVSIVQEKVDAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 77 RDIGRYMDTKVAEVYGG---MPYKaqinRVRNADIVVATPGRLLDLWSKGVIDLSSFEI--VIIDEADLMFE--MGFIDD 149
Cdd:cd18026 83 SPLFEELGFRVEGYAGNkgrSPPK----RRKSLSVAVCTIEKANSLVNSLIEEGRLDELglVVVDELHMLGDghRGALLE 158
|
170 180
....*....|....*....|....*
2Z0M_A 150 I---KIILAQTSNRKITGLfSATIP 171
Cdd:cd18026 159 LlltKLLYAAQKNIQIVGM-SATLP 182
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
18-325 |
2.43e-03 |
|
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: 39.68 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 18 TEVQSKTIPLMLQGKNVVV-RAKTGSGKT-AAYAIpILEL----GMKSLVVT-PTRELTRQVASHIRDIGrymDTKVAEV 90
Cdd:COG1203 133 NEALELALEAAEEEPGLFIlTAPTGGGKTeAALLF-ALRLaakhGGRRIIYAlPFTSIINQTYDRLRDLF---GEDVLLH 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 91 YG---------GMPYKAQINRVRN------ADIVVATPGRLLD-LWSKGvidlSSFE---------IVIIDEADlMFEmg 145
Cdd:COG1203 209 HSladldlleeEEEYESEARWLKLlkelwdAPVVVTTIDQLFEsLFSNR----KGQErrlhnlansVIILDEVQ-AYP-- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 146 fIDDIKIILAQTSNRKITG----LFSATIPEEIRKVVKD---FITNyEEIEACIGLANVEHKFVHVKD---DWRSKVQAL 215
Cdd:COG1203 282 -PYMLALLLRLLEWLKNLGgsviLMTATLPPLLREELLEayeLIPD-EPEELPEYFRAFVRKRVELKEgplSDEELAELI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 216 RENKDKGVIVFVRtRNRVAKLVRLFDNAIELRGD---------LPQSVRNRNI----DAFREGEYDMLITTDVASRGLDi 282
Cdd:COG1203 360 LEALHKGKSVLVI-VNTVKDAQELYEALKEKLPDeevyllhsrFCPADRSEIEkeikERLERGKPCILVSTQVVEAGVD- 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
2Z0M_A 283 plvekvINFD------APQDLrtYIHRIGRTGRMGRKG-EAITFILNEYW 325
Cdd:COG1203 438 ------IDFDvvirdlAPLDS--LIQRAGRCNRHGRKEeEGNVYVFDPED 479
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
13-192 |
3.07e-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: 38.51 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 13 GFKNFTEVQSKTIPLMLQGK-NVVVRAKTGSGKTAAYAIPIL-ELG---------------------MKSLVVTPTRELT 69
Cdd:cd18019 14 GFKSLNRIQSKLFPAAFETDeNLLLCAPTGAGKTNVALLTILrEIGkhrnpdgtinldafkivyiapMKALVQEMVGNFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 70 RQVASHirdigrymDTKVAEVYGGMPY-KAQINrvrNADIVVATPGRlLDLWSKGVIDLSSFEIV---IIDEADLMFemg 145
Cdd:cd18019 94 KRLAPY--------GITVAELTGDQQLtKEQIS---ETQIIVTTPEK-WDIITRKSGDRTYTQLVrliIIDEIHLLH--- 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
2Z0M_A 146 fiDD----IKIILAQTSNR--------KITGLfSATIPeeirkvvkdfitNYEEIEACI 192
Cdd:cd18019 159 --DDrgpvLESIVARTIRQieqtqeyvRLVGL-SATLP------------NYEDVATFL 202
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
29-137 |
3.42e-03 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 38.23 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 29 LQGKNVVVRAKTGSGKT--AAYAI-------PILELGMKSLVVTPTRELTRQvasHIRDIGRYMDT--KVAEVYGGMPYK 97
Cdd:cd18036 15 LRGKNTIICAPTGSGKTrvAVYICrhhlekrRSAGEKGRVVVLVNKVPLVEQ---QLEKFFKYFRKgyKVTGLSGDSSHK 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
2Z0M_A 98 ---AQInrVRNADIVVATPGRLLDLWSKGVID----LSSFEIVIIDE 137
Cdd:cd18036 92 vsfGQI--VKASDVIICTPQILINNLLSGREEervyLSDFSLLIFDE 136
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
248-337 |
4.00e-03 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 37.32 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 248 GDLPQSVRNRNIDAFREGEYDMLITTDVASRGLDIPLVEKVINFDAPQDLRTYIHRI-GRTGRMGRKGEAitfilneYWL 326
Cdd:cd18810 59 GQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKERAYA-------YFL 131
|
90
....*....|.
2Z0M_A 327 EKEVKKVSQKA 337
Cdd:cd18810 132 YPDQKKLTEDA 142
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
40-138 |
6.07e-03 |
|
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: 36.51 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2Z0M_A 40 TGSGKTA-AYAIPILELGMKSLVVTPTRELTRQVASHIRDigrYMDTKVAEVYGGMPYKAQInrvrNADIVVATPgRLLD 118
Cdd:cd17926 27 TGSGKTLtALALIAYLKELRTLIVVPTDALLDQWKERFED---FLGDSSIGLIGGGKKKDFD----DANVVVATY-QSLS 98
|
90 100
....*....|....*....|.
2Z0M_A 119 LWSKGVIDLSS-FEIVIIDEA 138
Cdd:cd17926 99 NLAEEEKDLFDqFGLLIVDEA 119
|
|
| |
