|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
57-403 |
9.62e-113 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 339.05 E-value: 9.62e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 57 LCENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQLHVPGGYRAIIVAPTRELCEQIYRQAE 136
Cdd:COG0513 13 LLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQALILAPTRELALQVAEELR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 137 KLSFGTSLKIIELS-KSNEKIQEKApkLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPGFIEQTDHIL 214
Cdd:COG0513 93 KLAKYLGLRVATVYgGVSIGRQIRA--LKRGVDIVVATPGRLLDLIERGaLDLSGVETLVLDEADRMLDMGFIEDIERIL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 215 SACTSS--NIcksLFSATIPSRVEELAKVVTVDPIRIIVGLKDAATDSIDQRLLFVGSDTsKIVILRQMISNGELKpRVV 292
Cdd:COG0513 171 KLLPKErqTL---LFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRD-KLELLRRLLRDEDPE-RAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 293 IFVQDIERAKALYTELLFDEIHVGVIHGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQSVHSY 372
Cdd:COG0513 246 VFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPEDPEDY 325
|
330 340 350
....*....|....*....|....*....|.
gi 19113945 373 IHRIGRTGRAGNTGQAVTFFTKEDGEYIKLI 403
Cdd:COG0513 326 VHRIGRTGRAGAEGTAISLVTPDERRLLRAI 356
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
57-252 |
3.94e-104 |
|
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: 308.75 E-value: 3.94e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 57 LCENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQLH-VPGGYRAIIVAPTRELCEQIYRQA 135
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPrKKKGLRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 136 EKLSFGTSLKIIELSKSNEKIQEKAPKLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPGFIEQTDHIL 214
Cdd:cd17957 81 LKLSKGTGLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGpIDLSSVEYLVLDEADKLFEPGFREQTDEIL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 19113945 215 SACTSSNICKSLFSATIPSRVEELAKVVTVDPIRIIVG 252
Cdd:cd17957 161 AACTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
57-391 |
1.85e-68 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 225.21 E-value: 1.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 57 LCENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQLH---VPGGYRAIIVAPTRELCEQIYR 133
Cdd:PRK11192 12 LLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFprrKSGPPRILILTPTRELAMQVAD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 134 QAEKLSFGTSLKIIelsksneKI------QEKAPKLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPGF 206
Cdd:PRK11192 92 QARELAKHTHLDIA-------TItggvayMNHAEVFSENQDIVVATPGRLLQYIKEEnFDCRAVETLILDEADRMLDMGF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 207 IEQTDHIlSACTSSNICKSLFSATIPSR-VEELAKVVTVDPIRIivglkDAATD-----SIDQRLLFVGSDTSKIVILRQ 280
Cdd:PRK11192 165 AQDIETI-AAETRWRKQTLLFSATLEGDaVQDFAERLLNDPVEV-----EAEPSrrerkKIHQWYYRADDLEHKTALLCH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 281 MISNGELKpRVVIFVQDIERAKALYTELLFDEIHVGVIHGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMV 360
Cdd:PRK11192 239 LLKQPEVT-RSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHV 317
|
330 340 350
....*....|....*....|....*....|.
gi 19113945 361 INFDFPQSVHSYIHRIGRTGRAGNTGQAVTF 391
Cdd:PRK11192 318 INFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
11-415 |
8.01e-63 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 213.48 E-value: 8.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 11 VKF-KN-KVPQPSIKEKEAKKLQGITKGKaKVT---GNN---PVDPIEE--FPEGILcENLKKQNITECTTIQRYAIPTI 80
Cdd:PTZ00110 87 VPFeKNfYKEHPEVSALSSKEVDEIRKEK-EITiiaGENvpkPVVSFEYtsFPDYIL-KSLKNAGFTEPTPIQVQGWPIA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 81 GSKRDLLACAPTGSGKTIAYLFP----ILQKLQLHVPGGYRAIIVAPTRELCEQIYRQAekLSFGTSLKIielskSNEKI 156
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPaivhINAQPLLRYGDGPIVLVLAPTRELAEQIREQC--NKFGASSKI-----RNTVA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 157 QEKAPK------LREKYDMCIGTPMRLVQAIQTGLS-FEKVEFFVMDEADRLFEPGFIEQTDHILSACTSSNIcKSLFSA 229
Cdd:PTZ00110 238 YGGVPKrgqiyaLRRGVEILIACPGRLIDFLESNVTnLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDRQ-TLMWSA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 230 TIPSRVEELAK-VVTVDPIRIIVGLKD-AATDSIDQRLlFVGSDTSKIV----ILRQMISNGelkPRVVIFVQDIERAKA 303
Cdd:PTZ00110 317 TWPKEVQSLARdLCKEEPVHVNVGSLDlTACHNIKQEV-FVVEEHEKRGklkmLLQRIMRDG---DKILIFVETKKGADF 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 304 LYTELLFDEIHVGVIHGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQSVHSYIHRIGRTGRAG 383
Cdd:PTZ00110 393 LTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAG 472
|
410 420 430
....*....|....*....|....*....|..
gi 19113945 384 NTGQAVTFFTKEDGEYIKLIAGVMRSSGCEVP 415
Cdd:PTZ00110 473 AKGASYTFLTPDKYRLARDLVKVLREAKQPVP 504
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
57-249 |
1.13e-62 |
|
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: 202.29 E-value: 1.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 57 LCENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKL---QLHVPGGYRAIIVAPTRELCEQIYR 133
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLlpePKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 134 QAEKLSFGTSLKIIEL-SKSNEKIQEKApkLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPGFIEQTD 211
Cdd:cd00268 81 VARKLGKGTGLKVAAIyGGAPIKKQIEA--LKKGPDIVVGTPGRLLDLIERGkLDLSNVKYLVLDEADRMLDMGFEEDVE 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 19113945 212 HILSACtSSNICKSLFSATIPSRVEELAKVVTVDPIRI 249
Cdd:cd00268 159 KILSAL-PKDRQTLLFSATLPEEVKELAKKFLKNPVRI 195
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
40-415 |
3.06e-60 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 205.79 E-value: 3.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 40 VTGNNPVDPIEEF-----PEGILcENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQLHVPG 114
Cdd:PLN00206 111 VKGEAVPPPILSFsscglPPKLL-LNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTIRSG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 115 GYR------AIIVAPTRELCEQIYRQAEKLSFGTSLKIiELSKSNEKIQEKAPKLREKYDMCIGTPMRLVQAI-QTGLSF 187
Cdd:PLN00206 190 HPSeqrnplAMVLTPTRELCVQVEDQAKVLGKGLPFKT-ALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLsKHDIEL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 188 EKVEFFVMDEADRLFEPGFIEQTDHILSACTSSNICksLFSATIPSRVEELAKVVTVDPIRIIVGLKDAATDSIDQRLLF 267
Cdd:PLN00206 269 DNVSVLVLDEVDCMLERGFRDQVMQIFQALSQPQVL--LFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIW 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 268 VGSDTSKIVILRQMISNGELKPRVVIFVqdierAKALYTELLFDEIHV--GV----IHGELPQAKREEALAKFRKGEIWV 341
Cdd:PLN00206 347 VETKQKKQKLFDILKSKQHFKPPAVVFV-----SSRLGADLLANAITVvtGLkalsIHGEKSMKERREVMKSFLVGEVPV 421
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113945 342 LIATDLLARGIDFHGVKMVINFDFPQSVHSYIHRIGRTGRAGNTGQAVTFFTKEDGEYIKLIAGVMRSSGCEVP 415
Cdd:PLN00206 422 IVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIP 495
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
69-424 |
6.08e-60 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 203.99 E-value: 6.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 69 CTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLqLHVP-------GGYRAIIVAPTRELCEQIYRQAEKLSFG 141
Cdd:PRK01297 110 CTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQL-LQTPppkerymGEPRALIIAPTRELVVQIAKDAAALTKY 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 142 TSLKIIELSKSNEKIQEKAPkLREKY-DMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPGFIEQTDHILSACTS 219
Cdd:PRK01297 189 TGLNVMTFVGGMDFDKQLKQ-LEARFcDILVATPGRLLDFNQRGeVHLDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPR 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 220 SNICKSL-FSATIPSRVEELAKVVTVDPIRIIVGLKDAATDSIDQRLLFV-GSDTSKiviLRQMISNGELKPRVVIFVQD 297
Cdd:PRK01297 268 KEERQTLlFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVaGSDKYK---LLYNLVTQNPWERVMVFANR 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 298 IERAKALYTELLFDEIHVGVIHGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQSVHSYIHRIG 377
Cdd:PRK01297 345 KDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIG 424
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 19113945 378 RTGRAGNTGQAVTFFTKEDGEYIKLIAGVM-RSSGCEVPNWVMALPKP 424
Cdd:PRK01297 425 RTGRAGASGVSISFAGEDDAFQLPEIEELLgRKISCEMPPAELLKPVP 472
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
57-391 |
1.71e-58 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 202.49 E-value: 1.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 57 LCENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLqLHVPG-------GYRAIIVAPTRELCE 129
Cdd:PRK04537 20 LLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRL-LSRPAladrkpeDPRALILAPTRELAI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 130 QIYRQAEKlsFGTSLKI--------IELSKSNEKIQEKApklrekyDMCIGTPMRLVQAIQTG--LSFEKVEFFVMDEAD 199
Cdd:PRK04537 99 QIHKDAVK--FGADLGLrfalvyggVDYDKQRELLQQGV-------DVIIATPGRLIDYVKQHkvVSLHACEICVLDEAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 200 RLFEPGFIEQTDHIL----SACTSSNIcksLFSATIPSRVEELAKVVTVDPIRIIVGLKDAATDSIDQRLLFvGSDTSKI 275
Cdd:PRK04537 170 RMFDLGFIKDIRFLLrrmpERGTRQTL---LFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYF-PADEEKQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 276 VILRQMISNGElKPRVVIFVQD---IER-AKALytellfDE--IHVGVIHGELPQAKREEALAKFRKGEIWVLIATDLLA 349
Cdd:PRK04537 246 TLLLGLLSRSE-GARTMVFVNTkafVERvARTL------ERhgYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 19113945 350 RGIDFHGVKMVINFDFPQSVHSYIHRIGRTGRAGNTGQAVTF 391
Cdd:PRK04537 319 RGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
61-422 |
5.51e-57 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 195.80 E-value: 5.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 61 LKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQLHVPGG-----YRAIIVAPTRELCEQIYRQA 135
Cdd:PRK10590 16 VAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHAkgrrpVRALILTPTRELAAQIGENV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 136 EKLSfgTSLKIIELSK-SNEKIQEKAPKLREKYDMCIGTPMRLVQ-AIQTGLSFEKVEFFVMDEADRLFEPGFIEQTDHI 213
Cdd:PRK10590 96 RDYS--KYLNIRSLVVfGGVSINPQMMKLRGGVDVLVATPGRLLDlEHQNAVKLDQVEILVLDEADRMLDMGFIHDIRRV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 214 LSACTS--SNIcksLFSATIPSRVEELAKVVTVDPIRIIVGLKDAATDSIDQRLLFVgSDTSKIVILRQMISNGELKpRV 291
Cdd:PRK10590 174 LAKLPAkrQNL---LFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFV-DKKRKRELLSQMIGKGNWQ-QV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 292 VIFVQDIERAKALYTELLFDEIHVGVIHGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQSVHS 371
Cdd:PRK10590 249 LVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVNYELPNVPED 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 19113945 372 YIHRIGRTGRAGNTGQAVTFFTKEDGEYIKLIAGVMRSsgcEVPNwvMALP 422
Cdd:PRK10590 329 YVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKK---EIPR--IAIP 374
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
59-391 |
3.96e-56 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 192.49 E-value: 3.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 59 ENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYL---F------PILQKLQLHVPggyRAIIVAPTRELCE 129
Cdd:PRK04837 21 EALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLtatFhyllshPAPEDRKVNQP---RALIMAPTRELAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 130 QIYRQAEKLSFGTSLKIiELSKSNEKIQEKAPKLREKYDMCIGTPMRLVQAIQTGL-SFEKVEFFVMDEADRLFEPGFIE 208
Cdd:PRK04837 98 QIHADAEPLAQATGLKL-GLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHiNLGAIQVVVLDEADRMFDLGFIK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 209 QTDHILSACTSSNICKS-LFSATIPSRVEELAKVVTVDPIRIIVGLKDAATDSIdQRLLFVGSDTSKIVILRQMISNgEL 287
Cdd:PRK04837 177 DIRWLFRRMPPANQRLNmLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRI-KEELFYPSNEEKMRLLQTLIEE-EW 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 288 KPRVVIFVQDIERAKALYTELLFDEIHVGVIHGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQ 367
Cdd:PRK04837 255 PDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPD 334
|
330 340
....*....|....*....|....
gi 19113945 368 SVHSYIHRIGRTGRAGNTGQAVTF 391
Cdd:PRK04837 335 DCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
57-403 |
4.24e-55 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 190.78 E-value: 4.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 57 LCENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQlhvPGGYR--AIIVAPTRELCEQIYRQ 134
Cdd:PRK11776 15 LLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLD---VKRFRvqALVLCPTRELADQVAKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 135 AEKLSFGT-SLKIIELSkSNEKIQEKAPKLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPGFIEQTDH 212
Cdd:PRK11776 92 IRRLARFIpNIKVLTLC-GGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGtLDLDALNTLVLDEADRMLDMGFQDAIDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 213 ILSACTssnicKS----LFSATIPSRVEELAKVVTVDPIRIIVGLKDAATdSIDQRLLFVgSDTSKIVILRQMISngELK 288
Cdd:PRK11776 171 IIRQAP-----ARrqtlLFSATYPEGIAAISQRFQRDPVEVKVESTHDLP-AIEQRFYEV-SPDERLPALQRLLL--HHQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 289 PR-VVIFVQDIERAKALYTELLFDEIHVGVIHGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQ 367
Cdd:PRK11776 242 PEsCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELAR 321
|
330 340 350
....*....|....*....|....*....|....*.
gi 19113945 368 SVHSYIHRIGRTGRAGNTGQAVTFFTKEDGEYIKLI 403
Cdd:PRK11776 322 DPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAI 357
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
261-392 |
4.54e-53 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 175.00 E-value: 4.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 261 IDQRLLFVGSDTSKIVILRQMISNGElKPRVVIFVQDIERAKALYTELLFDEIHVGVIHGELPQAKREEALAKFRKGEIW 340
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLK-PGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVR 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 19113945 341 VLIATDLLARGIDFHGVKMVINFDFPQSVHSYIHRIGRTGRAGNTGQAVTFF 392
Cdd:cd18787 80 VLVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
56-240 |
9.78e-50 |
|
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: 169.20 E-value: 9.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 56 ILCENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKL---QLHVPGGYR------AIIVAPTRE 126
Cdd:cd17967 10 LLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledGPPSVGRGRrkaypsALILAPTRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 127 LCEQIYRQAEKLSFGTSLKIIEL----SKSNEKIQekapkLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRL 201
Cdd:cd17967 90 LAIQIYEEARKFSYRSGVRSVVVyggaDVVHQQLQ-----LLRGCDILVATPGRLVDFIERGrISLSSIKFLVLDEADRM 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 19113945 202 FEPGFIEQTDHILSACTSSNICKS---LFSATIPSRVEELAK 240
Cdd:cd17967 165 LDMGFEPQIRKIVEHPDMPPKGERqtlMFSATFPREIQRLAA 206
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
70-403 |
3.71e-49 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 173.47 E-value: 3.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 70 TTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQLHVpGGYRAIIVAPTRELCEQIyrQAEKLSFGTSLKI-IE 148
Cdd:PTZ00424 52 SAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLIDYDL-NACQALILAPTRELAQQI--QKVVLALGDYLKVrCH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 149 LSKSNEKIQEKAPKLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPGFIEQTDHILSAcTSSNICKSLF 227
Cdd:PTZ00424 129 ACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRhLRVDDLKLFILDEADEMLSRGFKGQIYDVFKK-LPPDVQVALF 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 228 SATIPSRVEELAKVVTVDPIRIIVGLKDAATDSIDQRLLFVGSDTSKIVILRQMISNGELKpRVVIFVQDIERAKALYTE 307
Cdd:PTZ00424 208 SATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETLTIT-QAIIYCNTRRKVDYLTKK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 308 LLFDEIHVGVIHGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQSVHSYIHRIGRTGRAGNTGQ 387
Cdd:PTZ00424 287 MHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGV 366
|
330
....*....|....*.
gi 19113945 388 AVTFFTKEDGEYIKLI 403
Cdd:PTZ00424 367 AINFVTPDDIEQLKEI 382
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
57-249 |
3.62e-47 |
|
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: 162.09 E-value: 3.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 57 LCENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQLHVP-GGYRAIIVAPTRELCEQIYRQA 135
Cdd:cd17959 12 LLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPtVGARALILSPTRELALQTLKVT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 136 EKLSFGTSLKIIELSkSNEKIQEKAPKLREKYDMCIGTPMRLVQ-AIQTGLSFEKVEFFVMDEADRLFEPGFIEQTDHIL 214
Cdd:cd17959 92 KELGKFTDLRTALLV-GGDSLEEQFEALASNPDIIIATPGRLLHlLVEMNLKLSSVEYVVFDEADRLFEMGFAEQLHEIL 170
|
170 180 190
....*....|....*....|....*....|....*
gi 19113945 215 SACTSSNICkSLFSATIPSRVEELAKVVTVDPIRI 249
Cdd:cd17959 171 SRLPENRQT-LLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
70-238 |
1.56e-46 |
|
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: 158.94 E-value: 1.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 70 TTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQlHVPGGYRAIIVAPTRELCEQIYRQAEKLSFGTSLKIIEL 149
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD-KLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 150 sKSNEKIQEKAPKLReKYDMCIGTPMRLVQAIQTGLSFEKVEFFVMDEADRLFEPGFIEQTDHILSACtSSNICKSLFSA 229
Cdd:pfam00270 80 -LGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQERKLLKNLKLLVLDEAHRLLDMGFGPDLEEILRRL-PKKRQILLLSA 156
|
....*....
gi 19113945 230 TIPSRVEEL 238
Cdd:pfam00270 157 TLPRNLEDL 165
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
18-239 |
2.97e-44 |
|
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350810 [Multi-domain] Cd Length: 264 Bit Score: 156.28 E-value: 2.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 18 PQPSIKEKE--AKKLQGITKGK-----AKVTGNNPVDPIEEFPEGILCE----NLKKQNITECTTIQRYAIPTIGSKRDL 86
Cdd:cd18052 4 PPPPEDEDEifATIQTGINFDKydeipVEVTGRNPPPAILTFEEANLCEtllkNIRKAGYEKPTPVQKYAIPIILAGRDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 87 LACAPTGSGKTIAYLFPILQKL-----------QLHVPggyRAIIVAPTRELCEQIYRQAEKLSFGTSLKIIEL----SK 151
Cdd:cd18052 84 MACAQTGSGKTAAFLLPVLTGMmkegltassfsEVQEP---QALIVAPTRELANQIFLEARKFSYGTCIRPVVVyggvSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 152 SNEKIQekapkLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPGFIEQTDHILSAC--TSSNICKSL-F 227
Cdd:cd18052 161 GHQIRQ-----IEKGCHILVATPGRLLDFIGRGkISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPgmPSKEDRQTLmF 235
|
250
....*....|..
gi 19113945 228 SATIPSRVEELA 239
Cdd:cd18052 236 SATFPEEIQRLA 247
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
72-416 |
1.20e-40 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 154.24 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 72 IQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKL--QLHVPggyRAIIVAPTRELCEQIyrqAEKLS-FGTSLK--- 145
Cdd:PRK11634 32 IQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLdpELKAP---QILVLAPTRELAVQV---AEAMTdFSKHMRgvn 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 146 IIELSKSNE-KIQEKApkLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPGFIEQTDHILSACTSSNIc 223
Cdd:PRK11634 106 VVALYGGQRyDVQLRA--LRQGPQIVVGTPGRLLDHLKRGtLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQIPEGHQ- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 224 KSLFSATIPSRVEELAKVVTVDPIRIIVGLKDAATDSIDQRLLFVGSDTSKIVILRQMisNGELKPRVVIFVQD----IE 299
Cdd:PRK11634 183 TALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFL--EAEDFDAAIIFVRTknatLE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 300 RAKAL----YTEllfdeihvGVIHGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQSVHSYIHR 375
Cdd:PRK11634 261 VAEALerngYNS--------AALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHR 332
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 19113945 376 IGRTGRAGNTGQAVTFFTKEDGEYIKLIAGVMRSSGCEV--PN 416
Cdd:PRK11634 333 IGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVelPN 375
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
61-264 |
2.77e-40 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 143.79 E-value: 2.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 61 LKKQNITECTTIQRYAIPTI-GSKRDLLACAPTGSGKTIAYLFPILQKLQLHvpGGYRAIIVAPTRELCEQIYRQAEKLS 139
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALlSGLRDVILAAPTGSGKTLAALLPALEALKRG--KGGRVLVLVPTRELAEQWAEELKKLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 140 FGTSLKIIELSKSNEKIQEKAPKLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPGFIEQTDHILSACt 218
Cdd:smart00487 79 PSLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDkLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLL- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 19113945 219 SSNICKSLFSATIPSRVEELAKVVTVDPIRIIVGlkDAATDSIDQR 264
Cdd:smart00487 158 PKNVQLLLLSATPPEEIENLLELFLNDPVFIDVG--FTPLEPIEQF 201
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
57-254 |
5.52e-39 |
|
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: 141.35 E-value: 5.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 57 LCENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKL--QLHVPGGY----RAIIVAPTRELCEQ 130
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrYKLLAEGPfnapRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 131 IYRQAEKLSFGTSLKIIELSKSNEKIQEKAPKlREKYDMCIGTPMRLVQAIQTGL-SFEKVEFFVMDEADRLFEPGFIEQ 209
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGGRTKRQIRNPH-FEEVDILVATPGALSKLLTSRIySLEQLRHLVLDEADTLLDDSFNEK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19113945 210 TDHILSAC---------TSSNICKS---LFSATIPSRVEE-LAKVVTVDPIRIIVGLK 254
Cdd:cd17948 160 LSHFLRRFplasrrsenTDGLDPGTqlvLVSATMPSGVGEvLSKVIDVDSIETVTSDK 217
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
61-249 |
2.65e-38 |
|
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: 138.16 E-value: 2.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 61 LKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLqLHVPGGY---RAIIVAPTRELCEQIYRQAEK 137
Cdd:cd17947 5 LSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERL-LYRPKKKaatRVLVLVPTRELAMQCFSVLQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 138 LS-FG---TSLKIIELSKsneKIQEKApkLREKYDMCIGTPMRLVQAIQTGLSF--EKVEFFVMDEADRLFEPGFIEQTD 211
Cdd:cd17947 84 LAqFTditFALAVGGLSL---KAQEAA--LRARPDIVIATPGRLIDHLRNSPSFdlDSIEILVLDEADRMLEEGFADELK 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 19113945 212 HILSACtSSNICKSLFSATIPSRVEELAKVVTVDPIRI 249
Cdd:cd17947 159 EILRLC-PRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
61-247 |
3.30e-38 |
|
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: 138.10 E-value: 3.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 61 LKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLqLH------VPGGYRAIIVAPTRELCEQIYRQ 134
Cdd:cd17961 9 IAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKI-LKakaesgEEQGTRALILVPTRELAQQVSKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 135 AEKLSFGTS--LKIIELSkSNEKIQEKAPKLREKYDMCIGTPMRLVQAIQTG--LSFEKVEFFVMDEADRLFEPGFIEqt 210
Cdd:cd17961 88 LEQLTAYCRkdVRVVNLS-ASSSDSVQRALLAEKPDIVVSTPARLLSHLESGslLLLSTLKYLVIDEADLVLSYGYEE-- 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 19113945 211 DHILSACTSSNICKS-LFSATIPSRVEELAKVVTVDPI 247
Cdd:cd17961 165 DLKSLLSYLPKNYQTfLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
57-249 |
1.08e-37 |
|
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: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 57 LCENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFP----ILQKLQLHVPGGYRAIIVAPTRELCEQIY 132
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPmlvhIMDQRELEKGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 133 RQAEKLSFGTSLKIIELSKSNEKiQEKAPKLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPGFIEQTD 211
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSK-WEQAKALQEGAEIVVATPGRLIDMVKKKaTNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 19113945 212 HILSACTSSNICkSLFSATIPSRVEELAKVVTVDPIRI 249
Cdd:cd17952 160 SIVGHVRPDRQT-LLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
57-249 |
2.39e-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: 133.48 E-value: 2.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 57 LCENLK-KQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQLHVP-----GGYRAIIVAPTRELCEQ 130
Cdd:cd17949 1 LVSHLKsKMGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPrvdrsDGTLALVLVPTRELALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 131 IYRQAEKLsfgtsLK---------II--ELSKSnekiqEKApKLREKYDMCIGTPMRLVQAIQTGLSF--EKVEFFVMDE 197
Cdd:cd17949 81 IYEVLEKL-----LKpfhwivpgyLIggEKRKS-----EKA-RLRKGVNILIATPGRLLDHLKNTQSFdvSNLRWLVLDE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113945 198 ADRLFEPGFIEQTDHILSACTSSNI------------CKSLFSATIPSRVEELAKVVTVDPIRI 249
Cdd:cd17949 150 ADRLLDMGFEKDITKILELLDDKRSkaggekskpsrrQTVLVSATLTDGVKRLAGLSLKDPVYI 213
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
57-249 |
2.75e-36 |
|
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: 132.83 E-value: 2.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 57 LCENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLqLHVPGGYRAIIVAPTRELCEQIYRQAE 136
Cdd:cd17954 11 LCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQAL-LENPQRFFALVLAPTRELAQQISEQFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 137 KLSFGTSLKIIELSKSNEKIQEkAPKLREKYDMCIGTPMRLVQAIQT--GLSFEKVEFFVMDEADRLFEPGFIEQTDHIL 214
Cdd:cd17954 90 ALGSSIGLKSAVLVGGMDMMAQ-AIALAKKPHVIVATPGRLVDHLENtkGFSLKSLKFLVMDEADRLLNMDFEPEIDKIL 168
|
170 180 190
....*....|....*....|....*....|....*
gi 19113945 215 SAcTSSNICKSLFSATIPSRVEELAKVVTVDPIRI 249
Cdd:cd17954 169 KV-IPRERTTYLFSATMTTKVAKLQRASLKNPVKI 202
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
39-240 |
7.75e-36 |
|
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: 133.24 E-value: 7.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 39 KVTGNNPVDPIEEFPEGILCE----NLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPIL--------Q 106
Cdd:cd18051 10 EATGENCPPHIETFSDLDLGEiirnNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILsqiyeqgpG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 107 KLQLHVPGGYR-------AIIVAPTRELCEQIYRQAEKLSFGTSLKIIELSKSNEKIQEkapkLREKYDMC---IGTPMR 176
Cdd:cd18051 90 ESLPSESGYYGrrkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQ----MRDLERGChllVATPGR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113945 177 LVQAIQTG-LSFEKVEFFVMDEADRLFEPGFIEQTDHILSACTSSNICKS---LFSATIPSRVEELAK 240
Cdd:cd18051 166 LVDMLERGkIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERqtlMFSATFPKEIQMLAR 233
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
39-250 |
2.27e-34 |
|
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: 128.26 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 39 KVTGNNPVDPIEE-----FPEGILcENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQLHVP 113
Cdd:cd17953 1 KVRGKDCPKPIQKwsqcgLSEKVL-DLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 114 ----GGYRAIIVAPTRELCEQIYRQAEKLSFGTSLKIIELSKSNEkIQEKAPKLREKYDMCIGTPMRLVQAIQTG----L 185
Cdd:cd17953 80 vkpgEGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSG-ISEQIAELKRGAEIVVCTPGRMIDILTANngrvT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113945 186 SFEKVEFFVMDEADRLFEPGFIEQTDHILSACTSSNICkSLFSATIPSRVEELAKVVTVDPIRII 250
Cdd:cd17953 159 NLRRVTYVVLDEADRMFDMGFEPQIMKIVNNIRPDRQT-VLFSATFPRKVEALARKVLHKPIEIT 222
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
61-240 |
2.77e-34 |
|
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: 128.21 E-value: 2.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 61 LKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQlHVP--------GGYRAIIVAPTRELCEQIY 132
Cdd:cd17945 5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYIS-RLPpldeetkdDGPYALILAPTRELAQQIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 133 RQAEKLSFGTSLKIIELSkSNEKIQEKAPKLREKYDMCIGTPMRLVQAIQ-TGLSFEKVEFFVMDEADRLFEPGFIEQTD 211
Cdd:cd17945 84 EETQKFAKPLGIRVVSIV-GGHSIEEQAFSLRNGCEILIATPGRLLDCLErRLLVLNQCTYVVLDEADRMIDMGFEPQVT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 19113945 212 HILSACTSSNICKS-------------------LFSATIPSRVEELAK 240
Cdd:cd17945 163 KILDAMPVSNKKPDteeaeklaasgkhryrqtmMFTATMPPAVEKIAK 210
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
67-249 |
6.11e-34 |
|
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: 126.54 E-value: 6.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 67 TECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQ----LHVPGGYRAIIVAPTRELCEQIYRQAEKL--SF 140
Cdd:cd17960 11 TSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLkrkaNLKKGQVGALIISPTRELATQIYEVLQSFleHH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 141 GTSLKIIELSKSNEKIQEKAPKLREKYDMCIGTPMRL---VQAIQTGLSFEKVEFFVMDEADRLFEPGFIEQTDHILSAc 217
Cdd:cd17960 91 LPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLeelLSRKADKVKVKSLEVLVLDEADRLLDLGFEADLNRILSK- 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 19113945 218 tssnICKS----LFSATIPSRVEELAKVVTVDPIRI 249
Cdd:cd17960 170 ----LPKQrrtgLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
57-239 |
1.74e-33 |
|
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: 126.21 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 57 LCENLKKQNITECTTIQRYAIPTI---------GSKRDLLACAPTGSGKTIAYLFPILQKLQLHVPGGYRAIIVAPTREL 127
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLlpsskstppYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 128 CEQIYRQAEKLSFGTSLKIIELSKSNEKIQEK-------APKLREKYDMCIGTPMRLVQAIQ--TGLSFEKVEFFVMDEA 198
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQklllvdtSGRYLSRVDILVATPGRLVDHLNstPGFTLKHLRFLVIDEA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 199 DRLF-------------------EPGFIEQTDHILSACTSSNICKSLFSATIPSRVEELA 239
Cdd:cd17956 161 DRLLnqsfqdwletvmkalgrptAPDLGSFGDANLLERSVRPLQKLLFSATLTRDPEKLS 220
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
273-383 |
2.17e-33 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 121.93 E-value: 2.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 273 SKIVILRQMISNGElKPRVVIFVQDIERAKAlytELLFDE--IHVGVIHGELPQAKREEALAKFRKGEIWVLIATDLLAR 350
Cdd:pfam00271 1 EKLEALLELLKKER-GGKVLIFSQTKKTLEA---ELLLEKegIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAER 76
|
90 100 110
....*....|....*....|....*....|...
gi 19113945 351 GIDFHGVKMVINFDFPQSVHSYIHRIGRTGRAG 383
Cdd:pfam00271 77 GLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
57-240 |
5.48e-32 |
|
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: 121.18 E-value: 5.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 57 LCENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQLHvPGGYRAIIVAPTRELCEQIYRQAE 136
Cdd:cd17955 10 LVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSED-PYGIFALVLTPTRELAYQIAEQFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 137 KLSFGTSLKIIELSKSNEKIQEkAPKLREKYDMCIGTPMRLVQAIQTGL----SFEKVEFFVMDEADRLFEPGFIEQTDH 212
Cdd:cd17955 89 ALGAPLGLRCCVIVGGMDMVKQ-ALELSKRPHIVVATPGRLADHLRSSDdttkVLSRVKFLVLDEADRLLTGSFEDDLAT 167
|
170 180
....*....|....*....|....*....
gi 19113945 213 ILSAC-TSSNICksLFSATIPSRVEELAK 240
Cdd:cd17955 168 ILSALpPKRQTL--LFSATLTDALKALKE 194
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
61-242 |
1.61e-30 |
|
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: 117.68 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 61 LKKQNITECTTIQRYAI-PTIGSKRDLLACAPTGSGKTIAYLFPILQKL----QLHVPGGYRAIIVAPTRELCEQIYRQA 135
Cdd:cd17964 9 LTRMGFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLPAIQSLlntkPAGRRSGVSALIISPTRELALQIAAEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 136 EKL-SFGTSLKIIEL-SKSNEKIQEKAPKlREKYDMCIGTPMRLVQAIQ---TGLSFEKVEFFVMDEADRLFEPGF---I 207
Cdd:cd17964 89 KKLlQGLRKLRVQSAvGGTSRRAELNRLR-RGRPDILVATPGRLIDHLEnpgVAKAFTDLDYLVLDEADRLLDMGFrpdL 167
|
170 180 190
....*....|....*....|....*....|....*
gi 19113945 208 EQTDHILSACTSSNICKSLFSATIPSRVEELAKVV 242
Cdd:cd17964 168 EQILRHLPEKNADPRQTLLFSATVPDEVQQIARLT 202
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
61-251 |
4.24e-30 |
|
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: 115.85 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 61 LKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLqlhvpggYR----------AIIVAPTRELCEQ 130
Cdd:cd17941 5 LKEAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKL-------YRerwtpedglgALIISPTRELAMQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 131 IYRQAEKL----SFGTSLKI--IELSKSNEKIQEKapklrekyDMCIGTPMRLVQAIQ--TGLSFEKVEFFVMDEADRLF 202
Cdd:cd17941 78 IFEVLRKVgkyhSFSAGLIIggKDVKEEKERINRM--------NILVCTPGRLLQHMDetPGFDTSNLQMLVLDEADRIL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19113945 203 EPGFIEQTDHILsactsSNICKS----LFSATIPSRVEELAKVVTVDPIRIIV 251
Cdd:cd17941 150 DMGFKETLDAIV-----ENLPKSrqtlLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
61-241 |
7.63e-30 |
|
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: 115.15 E-value: 7.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 61 LKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFP---ILQKLQLHVPGGYRAIIVAPTRELCEQIYRQAEK 137
Cdd:cd17942 5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPaieLLYKLKFKPRNGTGVIIISPTRELALQIYGVAKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 138 L-SFGTSLKIIELSKSNEKIQekAPKLREKYDMCIGTPMRLVQAIQ--TGLSFEKVEFFVMDEADRLFEPGFIEQTDHIL 214
Cdd:cd17942 85 LlKYHSQTFGIVIGGANRKAE--AEKLGKGVNILVATPGRLLDHLQntKGFLYKNLQCLIIDEADRILEIGFEEEMRQII 162
|
170 180
....*....|....*....|....*..
gi 19113945 215 SaCTSSNICKSLFSATIPSRVEELAKV 241
Cdd:cd17942 163 K-LLPKRRQTMLFSATQTRKVEDLARI 188
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
304-383 |
1.15e-27 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 105.37 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 304 LYTELLFDEIHVGVIHGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQSVHSYIHRIGRTGRAG 383
Cdd:smart00490 3 LAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
57-250 |
1.52e-27 |
|
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: 108.79 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 57 LCENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQLHVPGGyRAIIVAPTRELCEQIYRQAE 136
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNP-SALILTPTRELAVQIEDQAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 137 KLSFGTSLKIIELSKSNEKIQEKAPKLREKYDMCIGTPMRLVQAI-QTGLSFEKVEFFVMDEADRLFEPGFIEQTDHILS 215
Cdd:cd17962 80 ELMKGLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILkQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 19113945 216 ACtsSNICKS-LFSATIPSRVEELAKVVTVDPIRII 250
Cdd:cd17962 160 NI--SHDHQTiLVSATIPRGIEQLAGQLLQNPVRIT 193
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
59-249 |
3.96e-27 |
|
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: 107.84 E-value: 3.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 59 ENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPIL---QKLQLHVPG-GYRAIIVAPTRELCEQIYRQ 134
Cdd:cd17966 3 DELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvhiNAQPPLERGdGPIVLVLAPTRELAQQIQQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 135 AEKlsFGTSLKIielskSNEKIQEKAPK------LREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPGFI 207
Cdd:cd17966 83 ANK--FGGSSRL-----RNTCVYGGAPKgpqirdLRRGVEICIATPGRLIDFLDQGkTNLRRVTYLVLDEADRMLDMGFE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 19113945 208 EQTDHILSAcTSSNICKSLFSATIPSRVEELAKVVTVDPIRI 249
Cdd:cd17966 156 PQIRKIVDQ-IRPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
72-392 |
5.17e-26 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 111.27 E-value: 5.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 72 IQRYAIPTIGSKRDLLACAPTGSGKTIAYLFpILQKLQLhvpgGYRAIIVAPTRELCEQIYRqaeklsfgtslkiiELSK 151
Cdd:COG1061 89 LEALLAALERGGGRGLVVAPTGTGKTVLALA-LAAELLR----GKRVLVLVPRRELLEQWAE--------------ELRR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 152 SNEKIQEKAPKLREKYDMCIGTPMRLVQAIQTGLSFEKVEFFVMDEADRLFEPGFIEQTDHI-------LSAcT-----S 219
Cdd:COG1061 150 FLGDPLAGGGKKDSDAPITVATYQSLARRAHLDELGDRFGLVIIDEAHHAGAPSYRRILEAFpaayrlgLTA-TpfrsdG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 220 SNICKSLFSATIPS-RVEELAK---VVTVDPIRIIVGLKD--AATDSIDQRL--LFVGSDTSKIVILRQMISNGELKPRV 291
Cdd:COG1061 229 REILLFLFDGIVYEySLKEAIEdgyLAPPEYYGIRVDLTDerAEYDALSERLreALAADAERKDKILRELLREHPDDRKT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 292 VIFVQDIERAKALYTELLFDEIHVGVIHGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQSVHS 371
Cdd:COG1061 309 LVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLRPTGSPRE 388
|
330 340
....*....|....*....|.
gi 19113945 372 YIHRIGRTGRAGNTGQAVTFF 392
Cdd:COG1061 389 FIQRLGRGLRPAPGKEDALVY 409
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
61-231 |
4.12e-25 |
|
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: 103.47 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 61 LKKQNITECTTIQRYAIP-TIGSKRDLLACAPTGSGKTIAYLFPILQKL--------QLHVPGGYRAIIVAPTRELCEQI 131
Cdd:cd17946 5 LADLGFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLlsqkssngVGGKQKPLRALILTPTRELAVQV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 132 YRQAEKLSFGTSLKIIEL--SKSNEKiQEKApkLREKYDMCIGTPMRLVQAIQTG----LSFEKVEFFVMDEADRLFEPG 205
Cdd:cd17946 85 KDHLKAIAKYTNIKIASIvgGLAVQK-QERL--LKKRPEIVVATPGRLWELIQEGnehlANLKSLRFLVLDEADRMLEKG 161
|
170 180 190
....*....|....*....|....*....|..
gi 19113945 206 FIEQTDHILSACTSSNICKS------LFSATI 231
Cdd:cd17946 162 HFAELEKILELLNKDRAGKKrkrqtfVFSATL 193
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
70-246 |
8.06e-25 |
|
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: 101.63 E-value: 8.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 70 TTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLqlhvpggyRAIIVAPTRELCEQIYRQAEKLS-FGTSLKIIE 148
Cdd:cd17938 23 TDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQIV--------VALILEPSRELAEQTYNCIENFKkYLDNPKLRV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 149 -LSKSNEKIQEKAPKLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPG---FIEQTDHILSACTSSN-- 221
Cdd:cd17938 95 aLLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGkLDLSSVRFFVLDEADRLLSQGnleTINRIYNRIPKITSDGkr 174
|
170 180
....*....|....*....|....*...
gi 19113945 222 --ICksLFSATIPS-RVEELAKVVTVDP 246
Cdd:cd17938 175 lqVI--VCSATLHSfEVKKLADKIMHFP 200
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
40-252 |
1.94e-24 |
|
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: 101.62 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 40 VTGNNPVDPIEEFPEGILCENL----KKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQlHVP-- 113
Cdd:cd18049 14 VRGHNCPKPVLNFYEANFPANVmdviARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHIN-HQPfl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 114 ---GGYRAIIVAPTRELCEQIYRQAEKLSFGTSLKiielSKSNEKIQEKAPKLRE---KYDMCIGTPMRLVQAIQTG-LS 186
Cdd:cd18049 93 ergDGPICLVLAPTRELAQQVQQVAAEYGRACRLK----STCIYGGAPKGPQIRDlerGVEICIATPGRLIDFLEAGkTN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113945 187 FEKVEFFVMDEADRLFEPGFIEQTDHILSACTSSNIcKSLFSATIPSRVEELAKVVTVDPIRIIVG 252
Cdd:cd18049 169 LRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQ-TLMWSATWPKEVRQLAEDFLKDYIHINIG 233
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
61-249 |
8.61e-24 |
|
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: 98.95 E-value: 8.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 61 LKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFP-ILQKLQ-------LHVPGGYrAIIVAPTRELCEQIY 132
Cdd:cd17951 5 LKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPlIMFALEqekklpfIKGEGPY-GLIVCPSRELARQTH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 133 ----RQAEKLSFGTSLKI-IELSKSNEKIQEKAPKLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPGF 206
Cdd:cd17951 84 evieYYCKALQEGGYPQLrCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKkINLDICRYLCLDEADRMIDMGF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19113945 207 IEQTDHILSACTSSNIcKSLFSATIPSRVEELAKVVTVDPIRI 249
Cdd:cd17951 164 EEDIRTIFSYFKGQRQ-TLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
70-250 |
3.71e-23 |
|
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: 96.62 E-value: 3.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 70 TTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKL--QLHVPggyRAIIVAPTRELCEQIYRQAEKLSFGTSLKII 147
Cdd:cd17939 21 SAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIdtTVRET---QALVLAPTRELAQQIQKVVKALGDYMGVKVH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 148 ELSkSNEKIQEKAPKLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPGFIEQTDHILSACTsSNICKSL 226
Cdd:cd17939 98 ACI-GGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRsLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLP-PETQVVL 175
|
170 180
....*....|....*....|....
gi 19113945 227 FSATIPSRVEELAKVVTVDPIRII 250
Cdd:cd17939 176 FSATMPHEVLEVTKKFMRDPVRIL 199
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
72-249 |
4.82e-23 |
|
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: 96.60 E-value: 4.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 72 IQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQLHVPgGYRAIIVAPTRELCEQIYRQAEKLSFGTSLKIIeLSK 151
Cdd:cd17940 25 IQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKD-VIQALILVPTRELALQTSQVCKELGKHMGVKVM-VTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 152 SNEKIQEKAPKLREKYDMCIGTPMRLVQAIQTGLS-FEKVEFFVMDEADRLFEPGFIEQTDHILSAC-TSSNICksLFSA 229
Cdd:cd17940 103 GGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVAdLSHCKTLVLDEADKLLSQDFQPIIEKILNFLpKERQIL--LFSA 180
|
170 180
....*....|....*....|
gi 19113945 230 TIPSRVEELAKVVTVDPIRI 249
Cdd:cd17940 181 TFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
35-252 |
5.50e-23 |
|
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: 98.16 E-value: 5.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 35 KGKAKVTGNNPVDPI-----EEFPEGILcENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQ 109
Cdd:cd18050 47 KKEITIRGVGCPKPVfafhqANFPQYVM-DVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVHIN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 110 lHVP-----GGYRAIIVAPTRELCEQIYRQAEKLSFGTSLKiielSKSNEKIQEKAPKLRE---KYDMCIGTPMRLVQAI 181
Cdd:cd18050 126 -HQPylergDGPICLVLAPTRELAQQVQQVADDYGKSSRLK----STCIYGGAPKGPQIRDlerGVEICIATPGRLIDFL 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113945 182 QTG-LSFEKVEFFVMDEADRLFEPGFIEQTDHILSACTSSNIcKSLFSATIPSRVEELAKVVTVDPIRIIVG 252
Cdd:cd18050 201 EAGkTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQ-TLMWSATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
72-250 |
3.97e-22 |
|
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: 94.05 E-value: 3.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 72 IQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQLHVPgGYRAIIVAPTRELCEQIYRQAEKLSFGTSLKiIELSK 151
Cdd:cd18046 25 IQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLK-ATQALVLAPTRELAQQIQKVVMALGDYMGIK-CHACI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 152 SNEKIQEKAPKLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPGFIEQTDHILSACTSSnICKSLFSAT 230
Cdd:cd18046 103 GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRRyLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQKLPPD-TQVVLLSAT 181
|
170 180
....*....|....*....|
gi 19113945 231 IPSRVEELAKVVTVDPIRII 250
Cdd:cd18046 182 MPNDVLEVTTKFMRDPIRIL 201
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
50-236 |
7.33e-21 |
|
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: 91.67 E-value: 7.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 50 EEFPEGILCENLKKQNITECTTIQRYAIPTI-----------------GSKRDLLAcAPTGSGKTIAYLFPILQKL---- 108
Cdd:cd17965 12 EAIIKEILKGSNKTDEEIKPSPIQTLAIKKLlktlmrkvtkqtsneepKLEVFLLA-AETGSGKTLAYLAPLLDYLkrqe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 109 -----------QLHV-PGGYRAIIVAPTRELCEQIYRQAEKLSFGTSLKIIELS-KSNEKIQEKAPKLREKYDMCIGTPM 175
Cdd:cd17965 91 qepfeeaeeeyESAKdTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSsGFGPSYQRLQLAFKGRIDILVTTPG 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113945 176 RLVQAIQTGLS-FEKVEFFVMDEADRLFEPGFIEQTDHILSACTSSNiCKSLFSATIPSRVE 236
Cdd:cd17965 171 KLASLAKSRPKiLSRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLK-HLILCSATIPKEFD 231
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
72-249 |
9.19e-21 |
|
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: 89.94 E-value: 9.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 72 IQRYAIPTIGSK--RDLLACAPTGSGKTIAYLFPILQKLQ--LHVPggyRAIIVAPTRELCEQIYRQAEKLSFGTSLKII 147
Cdd:cd17963 20 IQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDptLKSP---QALCLAPTRELARQIGEVVEKMGKFTGVKVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 148 ELSKSNekiqEKAPKLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEP-GFIEQTDHILSACTSSniCKS 225
Cdd:cd17963 97 LAVPGN----DVPRGKKITAQIVIGTPGTVLDWLKKRqLDLKKIKILVLDEADVMLDTqGHGDQSIRIKRMLPRN--CQI 170
|
170 180
....*....|....*....|....*
gi 19113945 226 -LFSATIPSRVEELAKVVTVDPIRI 249
Cdd:cd17963 171 lLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
59-249 |
2.46e-20 |
|
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: 88.68 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 59 ENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFP-----ILQKLQLHVPGGYRAIIVAPTRELCEQIYR 133
Cdd:cd17958 3 KEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgfihlDLQPIPREQRNGPGVLVLTPTRELALQIEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 134 QAEKLSFgTSLKIIEL---SKSNEKIQEkapkLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPGFIEQ 209
Cdd:cd17958 83 ECSKYSY-KGLKSVCVyggGNRNEQIED----LSKGVDIIIATPGRLNDLQMNNvINLKSITYLVLDEADRMLDMGFEPQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19113945 210 TDHILSACTSSNICkSLFSATIPSRVEELAKVVTVDPIRI 249
Cdd:cd17958 158 IRKILLDIRPDRQT-IMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
59-249 |
7.21e-20 |
|
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: 87.32 E-value: 7.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 59 ENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQLHVpGGYRAIIVAPTRELCEQI----YRQ 134
Cdd:cd17943 3 EGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLER-RHPQVLILAPTREIAVQIhdvfKKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 135 AEKL-SFGTSLKIIELSKSNEKIQEKAPKLrekydmCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFEPGFIEQTDH 212
Cdd:cd17943 82 GKKLeGLKCEVFIGGTPVKEDKKKLKGCHI------AVGTPGRIKQLIELGaLNVSHVRLFVLDEADKLMEGSFQKDVNW 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 19113945 213 ILSAcTSSNICKSLFSATIPSRVEELAKVVTVDPIRI 249
Cdd:cd17943 156 IFSS-LPKNKQVIAFSATYPKNLDNLLARYMRKPVLV 191
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
59-240 |
1.31e-18 |
|
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: 84.13 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 59 ENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQ-----LHVPGGYRAIIVAPTRELCEQIYR 133
Cdd:cd17944 3 KLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQedqqpRKRGRAPKVLVLAPTRELANQVTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 134 Q----AEKLSF-----GTSLkiielsksnekiQEKAPKLREKYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLFE 203
Cdd:cd17944 83 DfkdiTRKLSVacfygGTPY------------QQQIFAIRNGIDILVGTPGRIKDHLQNGrLDLTKLKHVVLDEVDQMLD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19113945 204 PGFIEQTDHILSAC----TSSNICKSLFSATIPSRVEELAK 240
Cdd:cd17944 151 MGFAEQVEEILSVSykkdSEDNPQTLLFSATCPDWVYNVAK 191
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
49-383 |
1.45e-15 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 79.17 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 49 IEEFPEGILCENLKKQNITECTTIQRYAIP-TIGSKRDLLACAPTGSGKT-IAYLFpILQklqlHVPGGYRAIIVAPTRE 126
Cdd:COG1204 3 VAELPLEKVIEFLKERGIEELYPPQAEALEaGLLEGKNLVVSAPTASGKTlIAELA-ILK----ALLNGGKALYIVPLRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 127 LCEQIYRQAEKL--SFGtsLKIIELSKSNEkiqEKAPKLrEKYDMCIGTPMRLVQAIQTGLSF-EKVEFFVMDEA----- 198
Cdd:COG1204 78 LASEKYREFKRDfeELG--IKVGVSTGDYD---SDDEWL-GRYDILVATPEKLDSLLRNGPSWlRDVDLVVVDEAhlidd 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 199 -DRlfepGFI-EQT-DHILSACTSSNIcksLF-SATIPSrVEELA-----KVVTVD--PIRIIVGLK------------- 254
Cdd:COG1204 152 eSR----GPTlEVLlARLRRLNPEAQI---VAlSATIGN-AEEIAewldaELVKSDwrPVPLNEGVLydgvlrfddgsrr 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 255 ------DAATDSID---QRLLFVGSDTS------KIVILRQMISNGELKPRVVIFVQDIERAKA--LYTELLFDEIHVGV 317
Cdd:COG1204 224 skdptlALALDLLEeggQVLVFVSSRRDaeslakKLADELKRRLTPEEREELEELAEELLEVSEetHTNEKLADCLEKGV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 318 I--HGELPQAKR---EEAlakFRKGEIWVLIATDLLARGI----------DFHGVKMVI--NFDFPQsvhsyihRIGRTG 380
Cdd:COG1204 304 AfhHAGLPSELRrlvEDA---FREGLIKVLVATPTLAAGVnlparrviirDTKRGGMVPipVLEFKQ-------MAGRAG 373
|
...
gi 19113945 381 RAG 383
Cdd:COG1204 374 RPG 376
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
66-251 |
8.84e-15 |
|
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: 73.15 E-value: 8.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 66 ITEC-----TTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQlHVPGGYRAIIVAPTRELCEQIYRQAEKLS- 139
Cdd:cd17950 17 IVDCgfehpSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLE-PVDGQVSVLVICHTRELAFQISNEYERFSk 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 140 FGTSLKI------IELSKSNEKIQEKAPklrekyDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEADRLfepgfIEQTD- 211
Cdd:cd17950 96 YMPNVKTavffggVPIKKDIEVLKNKCP------HIVVGTPGRILALVREKkLKLSHVKHFVLDECDKM-----LEQLDm 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 19113945 212 --HILSACTSSNICKS--LFSATIPSRVEELAKVVTVDPIRIIV 251
Cdd:cd17950 165 rrDVQEIFRATPHDKQvmMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
50-390 |
1.75e-14 |
|
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: 76.03 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 50 EEFPEGI---LCENLKKQNITECTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLqLHVPGGyRAIIVAPTRE 126
Cdd:COG1205 35 APWPDWLppeLRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEAL-LEDPGA-TALYLYPTKA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 127 LceqIYRQAEKLSfgtslKIIELSKSNEKI--------QEKAPKLREKYDMCIGTP-MrlvqaIQTGLS---------FE 188
Cdd:COG1205 113 L---ARDQLRRLR-----ELAEALGLGVRVatydgdtpPEERRWIREHPDIVLTNPdM-----LHYGLLphhtrwarfFR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 189 KVEFFVMDEA---------------DRLF--------EPGFIeqtdhilsaCTssnickslfSATI--PsrvEELA---- 239
Cdd:COG1205 180 NLRYVVIDEAhtyrgvfgshvanvlRRLRricrhygsDPQFI---------LA---------SATIgnP---AEHAerlt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 240 --KVVTVD----------------PIRIIVGLKDAATDSIDqrllfvgsdtskivILRQMISNGElkpRVVIFVQDIERA 301
Cdd:COG1205 239 grPVTVVDedgsprgertfvlwnpPLVDDGIRRSALAEAAR--------------LLADLVREGL---RTLVFTRSRRGA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 302 KALYTEL---LFDEIHVGVIH----GELPQAKRE-EalAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQSVHSYI 373
Cdd:COG1205 302 ELLARYArraLREPDLADRVAayraGYLPEERREiE--RGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFW 379
|
410
....*....|....*..
gi 19113945 374 HRIGRTGRAGNTGQAVT 390
Cdd:COG1205 380 QQAGRAGRRGQDSLVVL 396
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
50-250 |
2.21e-14 |
|
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: 71.73 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 50 EEFPEGILCENLKKQnitecTTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQLHVPgGYRAIIVAPTRELCE 129
Cdd:cd18045 8 EDLLRGIYAYGFEKP-----SAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVR-ETQALILSPTRELAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 130 QIyrQAEKLSFGTSLKI-IELSKSNEKIQEKAPKLREKYDMCIGTPMRLVQAIQ-TGLSFEKVEFFVMDEADRLFEPGFI 207
Cdd:cd18045 82 QI--QKVLLALGDYMNVqCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRrRSLRTRHIKMLVLDEADEMLNKGFK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 19113945 208 EQTDHI---LSACTSSnickSLFSATIPSRVEELAKVVTVDPIRII 250
Cdd:cd18045 160 EQIYDVyryLPPATQV----VLVSATLPQDILEMTNKFMTDPIRIL 201
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
70-198 |
2.52e-11 |
|
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: 62.28 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 70 TTIQRYAIPTIGSKRD-LLACAPTGSGKT-IAYLFpILQKLQLHvpgGYRAIIVAPTRELCEQIYRQ-AEKLSFGTSLKI 146
Cdd:cd17921 3 NPIQREALRALYLSGDsVLVSAPTSSGKTlIAELA-ILRALATS---GGKAVYIAPTRALVNQKEADlRERFGPLGKNVG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 19113945 147 IELSKSNEKIQEKApklreKYDMCIGTPMRLVQAIQTG--LSFEKVEFFVMDEA 198
Cdd:cd17921 79 LLTGDPSVNKLLLA-----EADILVATPEKLDLLLRNGgeRLIQDVRLVVVDEA 127
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
85-383 |
3.33e-11 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 64.78 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 85 DLLACAPTGSGKTIAYLfpILQKLQLHVPGGYRAIIVAPTRELCEQIYRQAEKLsFGTSLKIIELSKSNEKIQEK--APK 162
Cdd:TIGR01587 1 LLVIEAPTGYGKTEAAL--LWALHSIKSQKADRVIIALPTRATINAMYRRAKEL-FGSELVGLHHSSSFSRIKEMgdSEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 163 LREKYDMCIGTPMRLVQAIQT-----------GLSFEKVEF---------FVMDEADrLFEP---GFIEQTDHILSACTS 219
Cdd:TIGR01587 78 FEHLFPLYIHSNDKLFLDPITvctidqvlksvFGEFGHYEFtlasianslLIFDEVH-FYDEytlALILAVLEVLKDNDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 220 SNIcksLFSATIPSRVEELAKVVTVDPIRIIVGLKDAATDSIDQRLLFVGSDTSKIVILRQMISNGELKPRVVIFVQDIE 299
Cdd:TIGR01587 157 PIL---LMSATLPKFLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIESDKVGEISSLERLLEFIKKGGSIAIIVNTVD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 300 RAKALYTELLFD--EIHVGVIHGELPQAKRE----EALAKFRK-GEIWVLIATDLLARGIDfhgvkmvINFDF----PQS 368
Cdd:TIGR01587 234 RAQEFYQQLKEKapEEEIILYHSRFTEKDRAkkeaELLREMKKsNEKFVIVATQVIEASLD-------ISADVmiteLAP 306
|
330
....*....|....*
gi 19113945 369 VHSYIHRIGRTGRAG 383
Cdd:TIGR01587 307 IDSLIQRLGRLHRYG 321
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
83-198 |
5.56e-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: 61.90 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 83 KRDLLACAPTGSGKT-IAYLFpILQKLQL---HVPGGYRAIIVAPTRELCEQiyrQAEKLSFGTSLKIIELS-KSNEKIQ 157
Cdd:cd18034 16 KRNTIVVLPTGSGKTlIAVML-IKEMGELnrkEKNPKKRAVFLVPTVPLVAQ---QAEAIRSHTDLKVGEYSgEMGVDKW 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 19113945 158 EKAPKLRE--KYDMCIGTPMRLVQAIQTG-LSFEKVEFFVMDEA 198
Cdd:cd18034 92 TKERWKEEleKYDVLVMTAQILLDALRHGfLSLSDINLLIFDEC 135
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
85-201 |
8.19e-11 |
|
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: 60.11 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 85 DLLACAPTGSGKTIAYLFPILQKLqlhVPGGYRAIIVAPTRELCEQIYRQAEKLsFGTSLKIIELSkSNEKIQEKAPKLR 164
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLL---LKKGKKVLVLVPTKALALQTAERLREL-FGPGIRVAVLV-GGSSAEEREKNKL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 19113945 165 EKYDMCIGTPMRLVQAIQ--TGLSFEKVEFFVMDEADRL 201
Cdd:cd00046 78 GDADIIIATPDMLLNLLLreDRLFLKDLKLIIVDEAHAL 116
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
299-384 |
4.33e-10 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 58.04 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 299 ERAKALYTELLFdEIHvgviHGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQSVHSYIHRIGR 378
Cdd:cd18796 60 ELCPDRVPPDFI-ALH----HGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGR 134
|
....*.
gi 19113945 379 TGRAGN 384
Cdd:cd18796 135 SGHRPG 140
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
273-394 |
5.73e-10 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 61.67 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 273 SKIVILRQMIS---NGELKPRVVIFVQDIERAKALYTELLFDEIHVGVIHGE--------LPQAKREEALAKFRKGEIWV 341
Cdd:COG1111 335 PKLSKLREILKeqlGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNV 414
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 19113945 342 LIATDLLARGIDFHGVKMVINFDfPqsVHS---YIHRIGRTGRaGNTGQAVTFFTK 394
Cdd:COG1111 415 LVATSVAEEGLDIPEVDLVIFYE-P--VPSeirSIQRKGRTGR-KREGRVVVLIAK 466
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
85-383 |
8.71e-10 |
|
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: 60.14 E-value: 8.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 85 DLLACAPTGSGKTIAYLfpILQKLQLHVPGGYRAIIVAPTRELCEQIYRQAEKL--SFGTSLKIIELSKSNEKIQEKA-P 161
Cdd:cd09639 1 LLVIEAPTGYGKTEAAL--LWALHSLKSQKADRVIIALPTRATINAMYRRAKEAfgETGLYHSSILSSRIKEMGDSEEfE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 162 KLREKY----DMCIGTPMRLVQAIQTGLSFEK-VEFF------------VMDEADrLFEP---GFIEQTDHILSACTSSN 221
Cdd:cd09639 79 HLFPLYihsnDTLFLDPITVCTIDQVLKSVFGeFGHYeftlasiansllIFDEVH-FYDEytlALILAVLEVLKDNDVPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 222 IcksLFSATIPSRVEELAKVVTVDPIRIIVGLKDAATDSIDQRLLfvgSDTSKIVILRQMISNGELKPRVVIFVQDIERA 301
Cdd:cd09639 158 L---LMSATLPKFLKEYAEKIGYVEENEPLDLKPNERAPFIKIES---DKVGEISSLERLLEFIKKGGSVAIIVNTVDRA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 302 KALYTELLFD--EIHVGVIHGELPQA----KREEALAKFRKGEIWVLIATDLLARGIDfhgvkmvINFDF----PQSVHS 371
Cdd:cd09639 232 QEFYQQLKEKgpEEEIMLIHSRFTEKdrakKEAELLLEFKKSEKFVIVATQVIEASLD-------ISVDVmiteLAPIDS 304
|
330
....*....|..
gi 19113945 372 YIHRIGRTGRAG 383
Cdd:cd09639 305 LIQRLGRLHRYG 316
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
277-379 |
1.13e-09 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 60.62 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 277 ILRQMISNGElkpRVVIFVQDIERAKALYTELLFDEIHVGVIHGELPQAKREEALAKFRKG-EIWV-LIATDLLARGIDF 354
Cdd:COG0553 541 LLEELLAEGE---KVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGpEAPVfLISLKAGGEGLNL 617
|
90 100 110
....*....|....*....|....*....|..
gi 19113945 355 HGVKMVINFDFP-------QSVhSYIHRIGRT 379
Cdd:COG0553 618 TAADHVIHYDLWwnpaveeQAI-DRAHRIGQT 648
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
341-393 |
1.39e-09 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 54.25 E-value: 1.39e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 19113945 341 VLIATDLLARGIDFHGVKMVINFDFPQSVHSYIHRIGRTGRAGNTGQAVTFFT 393
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
319-396 |
3.27e-09 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 59.00 E-value: 3.27e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113945 319 HGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQSVHSYIHRIGRTGRAGNTGQAVTFFTKED 396
Cdd:COG0514 261 HAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPED 338
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
289-384 |
7.76e-09 |
|
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: 54.13 E-value: 7.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 289 PRVVIFVQDIERAKALY-----TELLFDEIHVGVI--HGELPQAKR--------EEALAKFRKGEIWVLIATDLLARGID 353
Cdd:cd18802 26 FRGIIFVERRATAVVLSrllkeHPSTLAFIRCGFLigRGNSSQRKRslmtqrkqKETLDKFRDGELNLLIATSVLEEGID 105
|
90 100 110
....*....|....*....|....*....|.
gi 19113945 354 FHGVKMVINFDFPQSVHSYIHRIGRtGRAGN 384
Cdd:cd18802 106 VPACNLVIRFDLPKTLRSYIQSRGR-ARAPN 135
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
262-392 |
9.14e-09 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 54.18 E-value: 9.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 262 DQRLLFVGSdTSKIVILRQMISNGELKPRVVIFVQDIERAKALYTELLfdeihVGVIHGELPQAKREEALAKFRKGEIWV 341
Cdd:cd18789 24 KRRLLAAMN-PNKLRALEELLKRHEQGDKIIVFTDNVEALYRYAKRLL-----KPFITGETPQSEREEILQNFREGEYNT 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 19113945 342 LIATDLLARGIDF--HGVKMVINFDFpQSVHSYIHRIGRTGRAGNTGQAVTFF 392
Cdd:cd18789 98 LVVSKVGDEGIDLpeANVAIQISGHG-GSRRQEAQRLGRILRPKKGGGKNAFF 149
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
90-345 |
9.44e-09 |
|
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: 57.40 E-value: 9.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 90 APTGSGKTIAYLFPILQKLQLHvpGGYRAIIVAPTRELCEQIYRQAEKLSFGT-----SLKIIELSKSNEKIQEKAPKLR 164
Cdd:COG1203 154 APTGGGKTEAALLFALRLAAKH--GGRRIIYALPFTSIINQTYDRLRDLFGEDvllhhSLADLDLLEEEEEYESEARWLK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 165 EK-----YDMCIGTPmrlVQAIQTGLS----FEKVeFF-------VMDEADrLFEPGFIEQTDHILSACTSSNiCKSLF- 227
Cdd:COG1203 232 LLkelwdAPVVVTTI---DQLFESLFSnrkgQERR-LHnlansviILDEVQ-AYPPYMLALLLRLLEWLKNLG-GSVILm 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 228 SATIPSRVEELAKvvtvDPIRIIVGLKDAATDSIDQ----RLLFVGSDTSKIVILRQMISNGELKPRVVIFVQDIERAKA 303
Cdd:COG1203 306 TATLPPLLREELL----EAYELIPDEPEELPEYFRAfvrkRVELKEGPLSDEELAELILEALHKGKSVLVIVNTVKDAQE 381
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 19113945 304 LYTEL--LFDEIHVGVIHGELPQAKR----EEALAKFRKGEIWVLIAT 345
Cdd:COG1203 382 LYEALkeKLPDEEVYLLHSRFCPADRseieKEIKERLERGKPCILVST 429
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
273-377 |
1.04e-08 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 53.63 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 273 SKIVILRQMISN-GELKPRVVIFVQDIERAKALYTELLFDEIHVGVIHGELPQAKREEALAKFRKG-EIWV-LIATDLLA 349
Cdd:cd18793 11 GKLEALLELLEElREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVfLLSTKAGG 90
|
90 100 110
....*....|....*....|....*....|....*
gi 19113945 350 RGIDFHGVKMVINFDFP-------QSVhSYIHRIG 377
Cdd:cd18793 91 VGLNLTAANRVILYDPWwnpaveeQAI-DRAHRIG 124
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
73-198 |
1.32e-08 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 54.51 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 73 QRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLqLHVPGGyRAIIVAPTRELceqIYRQAEKLS---FGTSLKI-IE 148
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEAL-LRDPGS-RALYLYPTKAL---AQDQLRSLRellEQLGLGIrVA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 19113945 149 LSKSNEKIQEKAPKLREKYDMCIGTPMRLVQAI-----QTGLSFEKVEFFVMDEA 198
Cdd:cd17923 80 TYDGDTPREERRAIIRNPPRILLTNPDMLHYALlphhdRWARFLRNLRYVVLDEA 134
|
|
| PRK10917 |
PRK10917 |
ATP-dependent DNA helicase RecG; Provisional |
93-345 |
2.72e-08 |
|
ATP-dependent DNA helicase RecG; Provisional
Pssm-ID: 236794 [Multi-domain] Cd Length: 681 Bit Score: 56.31 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 93 GSGKTIAYLFPILQKlqlhVPGGYRAIIVAPTRELCEQIYRQAEKL--SFGTSlkiIELSKSNEKIQEKAPKLRE----K 166
Cdd:PRK10917 292 GSGKTVVAALAALAA----IEAGYQAALMAPTEILAEQHYENLKKLlePLGIR---VALLTGSLKGKERREILEAiasgE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 167 YDMCIGTpmrlvQA-IQtglsfEKVEF----FVM-DEA--------DRLFEPGfieQTDHILsactssnicksLFSAT-I 231
Cdd:PRK10917 365 ADIVIGT-----HAlIQ-----DDVEFhnlgLVIiDEQhrfgveqrLALREKG---ENPHVL-----------VMTATpI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 232 PsRVeeLA-------KVVTVD-------PIRIIVgLKDAATDSIDQRLlfvgsdtskivilRQMISNGelkpRVVIFV-- 295
Cdd:PRK10917 421 P-RT--LAmtaygdlDVSVIDelppgrkPITTVV-IPDSRRDEVYERI-------------REEIAKG----RQAYVVcp 479
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 19113945 296 -------QDIERAKALYTEL--LFDEIHVGVIHGELPQAKREEALAKFRKGEIWVLIAT 345
Cdd:PRK10917 480 lieesekLDLQSAEETYEELqeAFPELRVGLLHGRMKPAEKDAVMAAFKAGEIDILVAT 538
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
319-392 |
7.89e-08 |
|
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: 51.06 E-value: 7.89e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113945 319 HGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQSVHSYIHRIGRTGRAGNTGQAVTFF 392
Cdd:cd18794 61 HAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
83-394 |
1.02e-07 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 54.49 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 83 KRDLLACAPTGSGKTIAYLFPILQKLqlHVPGGyRAIIVAPTRELCEQIYRQAEKLSFGTSLKIIELSKsneKIQ-EKAP 161
Cdd:PRK13766 29 KKNTLVVLPTGLGKTAIALLVIAERL--HKKGG-KVLILAPTKPLVEQHAEFFRKFLNIPEEKIVVFTG---EVSpEKRA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 162 KLREKYDMCIGTPmrlvQAIQTGL-----SFEKVEFFVMDEADR---------LFEPGFIEQTDHILSACTSS------- 220
Cdd:PRK13766 103 ELWEKAKVIVATP----QVIENDLiagriSLEDVSLLIFDEAHRavgnyayvyIAERYHEDAKNPLVLGLTASpgsdeek 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 221 --NICKSLFSATIPSRVEELAKV------VTVDPIRI-----IVGLKDAATDSIDQRL-----LFVGSDTSKIV------ 276
Cdd:PRK13766 179 ikEVCENLGIEHVEVRTEDDPDVkpyvhkVKIEWVRVelpeeLKEIRDLLNEALKDRLkklkeLGVIVSISPDVskkell 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 277 ----ILRQMISNGE-------------LK--------------------------------------------------- 288
Cdd:PRK13766 259 glqkKLQQEIANDDsegyeaisilaeaMKlrhavelletqgvealrrylerlreearssggskaskrlvedprfrkavrk 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 289 ---------------------------PRVVIFVQDIERAKALYTELLFDEIHVGVIHGelpQAKRE-----------EA 330
Cdd:PRK13766 339 akeldiehpkleklreivkeqlgknpdSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVG---QASKDgdkgmsqkeqiEI 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113945 331 LAKFRKGEIWVLIATDLLARGIDFHGVKMVInfdFPQSVHS---YIHRIGRTGRaGNTGQAVTFFTK 394
Cdd:PRK13766 416 LDKFRAGEFNVLVSTSVAEEGLDIPSVDLVI---FYEPVPSeirSIQRKGRTGR-QEEGRVVVLIAK 478
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
72-154 |
1.48e-07 |
|
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: 51.97 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 72 IQRYAIPTI-GSKRDLLACAPTGSGKTIAYLFPILQKLQ---LHVPGGYRAIIVAPTRELCEQIYRQ-AEKLSfGTSLKI 146
Cdd:cd18023 5 IQSEVFPDLlYSDKNFVVSAPTGSGKTVLFELAILRLLKernPLPWGNRKVVYIAPIKALCSEKYDDwKEKFG-PLGLSC 83
|
....*...
gi 19113945 147 IELSKSNE 154
Cdd:cd18023 84 AELTGDTE 91
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
73-213 |
1.91e-07 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 50.75 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 73 QRYAIPTI------GSKRDLLAcAPTGSGKTIAYLFPILQKLQLHvpGGYRAIIVAPTRELCEQIYRQAEKLsFGTSLKI 146
Cdd:pfam04851 8 QIEAIENLlesiknGQKRGLIV-MATGSGKTLTAAKLIARLFKKG--PIKKVLFLVPRKDLLEQALEEFKKF-LPNYVEI 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 147 IELSKSNEKIQEkapklREKYDMCIGTPMRLVQAIQTG---LSFEKVEFFVMDEADRLFEPGFIEQTDHI 213
Cdd:pfam04851 84 GEIISGDKKDES-----VDDNKIVVTTIQSLYKALELAsleLLPDFFDVIIIDEAHRSGASSYRNILEYF 148
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
290-381 |
2.03e-07 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 50.05 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 290 RVVIFVQDIERAKALYTELLFDE------IHVGVIHGE----LPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKM 359
Cdd:cd18801 32 RVIIFSEFRDSAEEIVNFLSKIRpgiratRFIGQASGKsskgMSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDL 111
|
90 100
....*....|....*....|..
gi 19113945 360 VINFDFPQSVHSYIHRIGRTGR 381
Cdd:cd18801 112 IICYDASPSPIRMIQRMGRTGR 133
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
295-383 |
2.68e-07 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 50.04 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 295 VQDIERAKALY---TELLFDEIHVGVIHGELPQAKREEALAKFRKGEIWVLIATDLLARGIDF-HGVKMVI----NFDFP 366
Cdd:cd18811 41 KLDLKAAVAMYeylKERFRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVpNATVMVIedaeRFGLS 120
|
90
....*....|....*...
gi 19113945 367 QsvhsyIHRI-GRTGRAG 383
Cdd:cd18811 121 Q-----LHQLrGRVGRGD 133
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
313-396 |
4.36e-07 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 52.41 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 313 IHVGVIHGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQSVHSYIHRIGRTGRAGNTGQAVTFF 392
Cdd:PRK11057 261 ISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFY 340
|
....
gi 19113945 393 TKED 396
Cdd:PRK11057 341 DPAD 344
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
70-246 |
5.11e-07 |
|
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: 50.79 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 70 TTIQRYAIPTIGSK--RDLLACAPTGSGKTIAYLFPILQKLQLH--VPggyRAIIVAPTRELCEQIYRQAEKL-SFGTSL 144
Cdd:cd18048 42 SKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRVDALklYP---QCLCLSPTFELALQTGKVVEEMgKFCVGI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 145 KIIELSKSNekiqeKAPK-LREKYDMCIGTP---------MRLVqaiqtglSFEKVEFFVMDEADRLFE-PGFIEQTDHI 213
Cdd:cd18048 119 QVIYAIRGN-----RPGKgTDIEAQIVIGTPgtvldwcfkLRLI-------DVTNISVFVLDEADVMINvQGHSDHSVRV 186
|
170 180 190
....*....|....*....|....*....|....
gi 19113945 214 LSACTSSniCKS-LFSATIPSRVEELAKVVTVDP 246
Cdd:cd18048 187 KRSMPKE--CQMlLFSATFEDSVWAFAERIVPDP 218
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
289-396 |
8.37e-07 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 48.80 E-value: 8.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 289 PRVV-IFVQDIERAKALYTEL--LFDEIHVGVIHGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVK-MVIN-- 362
Cdd:cd18792 34 PRIEeSEKLDLKSIEALAEELkeLVPEARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANtMIIEda 113
|
90 100 110
....*....|....*....|....*....|....*..
gi 19113945 363 --FDFPQsvhsyIHRI-GRTGRAGNtgQAVTFFTKED 396
Cdd:cd18792 114 drFGLSQ-----LHQLrGRVGRGKH--QSYCYLLYPD 143
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
54-200 |
1.21e-06 |
|
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: 48.57 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 54 EGILCENLKKQNITECTTIQRYAIPTI------GSKRDLLACAPTGSGKTIAYLFPILqklqLHVPGGYRAIIVAPTREL 127
Cdd:cd17918 1 DRALIQELCKSLPFSLTKDQAQAIKDIekdlhsPEPMDRLLSGDVGSGKTLVALGAAL----LAYKNGKQVAILVPTEIL 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113945 128 CEQIYRQAEKlsFGTSLKIIELSK-SNEKIQEKApklrekyDMCIGTPmrlvQAIQTGLSFEKVEFFVMDEADR 200
Cdd:cd17918 77 AHQHYEEARK--FLPFINVELVTGgTKAQILSGI-------SLLVGTH----ALLHLDVKFKNLDLVIVDEQHR 137
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
320-384 |
1.25e-06 |
|
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: 48.02 E-value: 1.25e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113945 320 GELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQSVHSYIHRIGRTGRAGN 384
Cdd:cd18797 74 AGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGK 138
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
286-392 |
1.32e-06 |
|
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: 50.64 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 286 ELKPRVVIFVQDIERAKALYTEL--LFDEIHVGVIHGELPQakREEALAKFRKGEIWVLIATDLLARGIDFHGVK-MVIN 362
Cdd:COG4098 317 KEGRQLLIFVPTIELLEQLVALLqkLFPEERIAGVHAEDPE--RKEKVQAFRDGEIPILVTTTILERGVTFPNVDvAVLG 394
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 19113945 363 FDfpqsvhsyiHRI----------GRTGRAGN--TGQaVTFF 392
Cdd:COG4098 395 AD---------HPVfteaalvqiaGRVGRSADypTGE-VIFF 426
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
84-146 |
3.24e-06 |
|
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: 47.19 E-value: 3.24e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113945 84 RDLLACAPTGSGKTIAYLFPILQKLQLHVPGGYRAIIVAPTRELCEQIYRQAEKLSFGTSLKI 146
Cdd:cd17922 2 RNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLEI 64
|
|
| DinG |
COG1199 |
Rad3-related DNA helicase DinG [Replication, recombination and repair]; |
79-195 |
3.29e-06 |
|
Rad3-related DNA helicase DinG [Replication, recombination and repair];
Pssm-ID: 440812 [Multi-domain] Cd Length: 629 Bit Score: 49.54 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 79 TIGSKRDLLACAPTGSGKTIAYLFPILqklqLHVP-GGYRAIIVAPTRELCEQIYRQA-EKLS--FGTSLKIIELsksne 154
Cdd:COG1199 29 ALAEGRHLLIEAGTGTGKTLAYLVPAL----LAAReTGKKVVISTATKALQEQLVEKDlPLLRkaLGLPLRVALL----- 99
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 19113945 155 kiqeKApklREKYdMCigtPMRLVQAIQTGLSFEKVEFFVM 195
Cdd:COG1199 100 ----KG---RSNY-LC---LRRLEQALQEGDDLDDEELLLA 129
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
70-108 |
3.99e-06 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 49.33 E-value: 3.99e-06
10 20 30
....*....|....*....|....*....|....*....
gi 19113945 70 TTIQRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKL 108
Cdd:COG1201 26 TPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDEL 64
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
267-396 |
4.77e-06 |
|
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: 46.57 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 267 FVGSDTSKIV---ILRQMISNGE---LKPRVvifvQDIERAKALYTELLfDEIHVGVIHGELPQAKREEALAKFRKGEIW 340
Cdd:cd18810 5 YVMPYDDELIreaIERELLRGGQvfyVHNRI----ESIEKLATQLRQLV-PEARIAIAHGQMTENELEEVMLEFAKGEYD 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 19113945 341 VLIATDLLARGIDFHGVKMVINFDFPQSVHSYIHRI-GRTGRAGNTGQAvtFFTKED 396
Cdd:cd18810 80 ILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKERAYA--YFLYPD 134
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
73-421 |
5.17e-06 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 49.17 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 73 QRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKLQlhvpGGYRAIIVAPTRELceqiyrqaeklsfgtslkiielskS 152
Cdd:COG4581 30 QEEAILALEAGRSVLVAAPTGSGKTLVAEFAIFLALA----RGRRSFYTAPIKAL------------------------S 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 153 NEKIQEkapkLREKY----------DMCIGTPMRLV---------QAIQTGLSFEKVEFFVMDEADRLFEPG-------- 205
Cdd:COG4581 82 NQKFFD----LVERFgaenvglltgDASVNPDAPIVvmtteilrnMLYREGADLEDVGVVVMDEFHYLADPDrgwvweep 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 206 FIEQTDHI----LSAcTSSNIckSLFSATIPSRVEELAKVVTVD---PIRIIVGLKDAATD--SIDQRLLFVgsdTSKIV 276
Cdd:COG4581 158 IIHLPARVqlvlLSA-TVGNA--EEFAEWLTRVRGETAVVVSEErpvPLEFHYLVTPRLFPlfRVNPELLRP---PSRHE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 277 ILRQMISNGELKPRVVIFVQD--IERAKAL-----------------------------YTELLFDEIH-VGVIH-GELP 323
Cdd:COG4581 232 VIEELDRGGLLPAIVFIFSRRgcDEAAQQLlsarlttkeeraeireaidefaedfsvlfGKTLSRLLRRgIAVHHaGMLP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 324 QAKR-EEALakFRKGEIWVLIATDLLARGID-------------FHGVKMVinfdfPQSVHSYiHRI-GRTGRAG--NTG 386
Cdd:COG4581 312 KYRRlVEEL--FQAGLLKVVFATDTLAVGINmpartvvftklskFDGERHR-----PLTAREF-HQIaGRAGRRGidTEG 383
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 19113945 387 QAVTFFTKEDG--EYIKLIAGV---MRSSGceVPNWVMAL 421
Cdd:COG4581 384 HVVVLAPEHDDpkKFARLASARpepLRSSF--RPSYNMVL 421
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
286-381 |
5.84e-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: 46.53 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 286 ELKPRVVIFVQdIERAKALYTELLFDEIHVGvIHGELPQAKREEALAKFRKGEIWVLIAT----DLLARGIDF-HGVKMV 360
Cdd:cd18798 22 KLGDGGLIFVS-IDYGKEYAEELKEFLERHG-IKAELALSSTEKNLEKFEEGEIDVLIGVasyyGVLVRGIDLpERIKYA 99
|
90 100
....*....|....*....|.
gi 19113945 361 INFDFPqsVHSYIHRIGRTGR 381
Cdd:cd18798 100 IFYGVP--VTTYIQASGRTSR 118
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
278-381 |
7.03e-06 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 46.47 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 278 LRQMISNGElkpRVVIFVQDIERAKALYTELLFDEIHVGVIHGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGV 357
Cdd:cd18790 20 IRKRVARGE---RVLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEV 96
|
90 100
....*....|....*....|....*....
gi 19113945 358 KMVINFD-----FPQSVHSYIHRIGRTGR 381
Cdd:cd18790 97 SLVAILDadkegFLRSETSLIQTIGRAAR 125
|
|
| RecG |
COG1200 |
RecG-like helicase [Replication, recombination and repair]; |
297-345 |
7.14e-06 |
|
RecG-like helicase [Replication, recombination and repair];
Pssm-ID: 440813 [Multi-domain] Cd Length: 684 Bit Score: 48.51 E-value: 7.14e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 19113945 297 DIERAKALYTEL--LFDEIHVGVIHGELPQAKREEALAKFRKGEIWVLIAT 345
Cdd:COG1200 486 DLQAAEETYEELreAFPGLRVGLLHGRMKPAEKDAVMAAFKAGEIDVLVAT 536
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
319-380 |
1.74e-05 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 47.61 E-value: 1.74e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113945 319 HGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQSVHSYIHRIGRTG 380
Cdd:PRK09751 308 HGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
84-197 |
2.08e-05 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 45.54 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 84 RDLLACAPTGSGKTIAYLFPILQKLQLHVPGGY--RAIIVAPTRELCEQiyrQAEKLS--FGTSLKIIELSKSnEKIQEK 159
Cdd:cd18036 18 KNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEkgRVVVLVNKVPLVEQ---QLEKFFkyFRKGYKVTGLSGD-SSHKVS 93
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 19113945 160 APKLREKYDMCIGTPMRLVQAIQTGLSFEKVEF-----FVMDE 197
Cdd:cd18036 94 FGQIVKASDVIICTPQILINNLLSGREEERVYLsdfslLIFDE 136
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
87-198 |
2.29e-05 |
|
C-terminal D[D/E]X[H/Q]-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: 350779 [Multi-domain] Cd Length: 191 Bit Score: 44.94 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 87 LACAPTGSGKTIAYLFPILQklQLHVPGGYRAIIVAPTRELCEQIYRQ-AEKLSFGTSLKIIELS---KSNEKIQEKApk 162
Cdd:cd18021 23 FVGAPTGSGKTVCAELALLR--HWRQNPKGRAVYIAPMQELVDARYKDwRAKFGPLLGKKVVKLTgetSTDLKLLAKS-- 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 19113945 163 lrekyDMCIGTPMRLVQ---------AIQTglsfekVEFFVMDEA 198
Cdd:cd18021 99 -----DVILATPEQWDVlsrrwkqrkNVQS------VELFIADEL 132
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
84-200 |
2.38e-05 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 45.12 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 84 RDLLACAPTGSGKT-IAYLfpILQKLQLHVPGGY--RAIIVAPTRELCEQIYRQAEKLSFGTSLKIIELSkSNEKIQEKA 160
Cdd:cd17927 18 KNTIICLPTGSGKTfVAVL--ICEHHLKKFPAGRkgKVVFLANKVPLVEQQKEVFRKHFERPGYKVTGLS-GDTSENVSV 94
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 19113945 161 PKLREKYDMCIGTPMRLVQAIQTG--LSFEKVEFFVMDEADR 200
Cdd:cd17927 95 EQIVESSDVIIVTPQILVNDLKSGtiVSLSDFSLLVFDECHN 136
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
73-133 |
3.15e-05 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 46.42 E-value: 3.15e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113945 73 QRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILQKL-QLHVPGG-----YrAIIVAPTRELCEQIYR 133
Cdd:PRK13767 37 QRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELfRLGREGEledkvY-CLYVSPLRALNNDIHR 102
|
|
| Cas3_I-D |
cd09710 |
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; ... |
90-380 |
3.72e-05 |
|
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Diverged DNA helicase Cas3'; signature gene for Type I and subtype I-D
Pssm-ID: 187841 [Multi-domain] Cd Length: 353 Bit Score: 45.63 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 90 APTGSGKTIAYLFPILQklqlhvpGGYRAIIVAPTRELCEQIYRQAEKL--SFGTSLKIIELSKSNEKIQEKAPKLREKY 167
Cdd:cd09710 21 APTGAGKTLAWLTPLLH-------GENKAIALYPTNALIEDQTEAIKEFvdDANPRHQVKSLSASDITLWPNDKNVGSSK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 168 DMCIGTPMRLVQAIQTGL--------------------------SFEKVEFFVMDEadrlFEPGFIEQTDHIL-----SA 216
Cdd:cd09710 94 GEKLYNLLRNDIGTSTPIilltnpdifvyltrfayidrgdiaagFYTKFSTVIFDE----FHLYDAKQLVGLLfylayMQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 217 CTSSNICKSLF---SATIPSRVE---ELAKVVTVdPIRIIVGLKDAATDsiDQRLLFVGSDTSKIVILRQM--------- 281
Cdd:cd09710 170 LIRFFECRRKFvflSATPDPALIlrlQNAKQAGV-KIAPIDGEAGQFPD--NPELEQQLKNTSFRPVLPPVelelipapd 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 282 ISNGELKPRVVIFVQDIERAKALYTELLFDEIH-----------------VGVIHGELPQAKREEALakfrkgEIWVLIA 344
Cdd:cd09710 247 FKEEWLAELAAEVIERFRQLPGERGAIILDSLDevnrlsdllqqqglgddIGRITGFAPKKDRERAM------QFDILLG 320
|
330 340 350
....*....|....*....|....*....|....*.
gi 19113945 345 TDLLARGIDFHGVKMVINfdfPQSVHSYIHRIGRTG 380
Cdd:cd09710 321 TSTVDVGVDFKRDWLIFS---ARDAAAFWQRLGRLG 353
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
72-199 |
4.85e-05 |
|
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: 44.24 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 72 IQRYAIPTIGSKRDLLACAPTGSGKTIaylFPILQKLQLHVPGGyRAIIVAPTRELCEQIYRQAEKLSFGTSLKIIEL-- 149
Cdd:cd17924 21 AQRTWAKRLLRGKSFAIIAPTGVGKTT---FGLATSLYLASKGK-RSYLIFPTKSLVKQAYERLSKYAEKAGVEVKILvy 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 19113945 150 -SKSNEKIQEKAPKLREK--YDMCIGTPMRLVQAIQTgLSFEKVEFFVMDEAD 199
Cdd:cd17924 97 hSRLKKKEKEELLEKIEKgdFDILVTTNQFLSKNFDL-LSNKKFDFVFVDDVD 148
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
319-402 |
6.23e-05 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 45.66 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 319 HGELPQAKREEALAKFRKGEIWVLIATDLLARGIDFHGVKMVINFDFPQSVHSYIHRIGRTGRAGNTGQAVTFFTKEDge 398
Cdd:PLN03137 711 HGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRAGRDGQRSSCVLYYSYSD-- 788
|
....
gi 19113945 399 YIKL 402
Cdd:PLN03137 789 YIRV 792
|
|
| DEXHc_RecG |
cd17992 |
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in ... |
93-200 |
8.29e-05 |
|
DEXH/Q-box helicase domain of RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. It is a member 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: 350750 [Multi-domain] Cd Length: 225 Bit Score: 44.06 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 93 GSGKTIAYLFPILQKLQlhvpGGYRAIIVAPTRELCEQIYRQAEKLSFGTSLKIIELS---KSNEKIQEKApKLRE-KYD 168
Cdd:cd17992 76 GSGKTVVAALAMLAAVE----NGYQVALMAPTEILAEQHYDSLKKLLEPLGIRVALLTgstKAKEKREILE-KIASgEID 150
|
90 100 110
....*....|....*....|....*....|...
gi 19113945 169 MCIGTpmrlvQA-IQTGLSFEKVEFFVMDEADR 200
Cdd:cd17992 151 IVIGT-----HAlIQEDVEFHNLGLVIIDEQHR 178
|
|
| DEXHc_cas3 |
cd17930 |
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ... |
86-233 |
8.57e-05 |
|
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350688 [Multi-domain] Cd Length: 186 Bit Score: 43.43 E-value: 8.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 86 LLACAPTGSGKTIAYLFPIlqkLQLHVPGGYRAIIVA-PTRELCEQIYRQAEKL--SFGTSLKIIEL-SKSNEKIQEKAP 161
Cdd:cd17930 4 VILEAPTGSGKTEAALLWA---LKLAARGGKRRIIYAlPTRATINQMYERIREIlgRLDDEDKVLLLhSKAALELLESDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 162 KLREK----------------YDMCIGTPmrlVQAIQTGLSFEKVEF---------FVMDEA----DRLFePGFIEQTDH 212
Cdd:cd17930 81 EPDDDpveavdwalllkrswlAPIVVTTI---DQLLESLLKYKHFERrlhglansvVVLDEVqaydPEYM-ALLLKALLE 156
|
170 180
....*....|....*....|.
gi 19113945 213 ILSACTSSNIcksLFSATIPS 233
Cdd:cd17930 157 LLGELGGPVV---LMTATLPA 174
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
83-200 |
1.50e-04 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 42.50 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 83 KRDLLACAPTGSGKTIAYLFPILQKLQLHvpgGYRAIIVAPTRELCEQIYRQAEKLsFGTSLKIIELSKsnekiqEKAPK 162
Cdd:cd18035 16 NGNTLIVLPTGLGKTIIAILVAADRLTKK---GGKVLILAPSRPLVEQHAENLKRV-LNIPDKITSLTG------EVKPE 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 19113945 163 LREK-YDMC---IGTPMRLVQAIQTG-LSFEKVEFFVMDEADR 200
Cdd:cd18035 86 ERAErWDASkiiVATPQVIENDLLAGrITLDDVSLLIFDEAHH 128
|
|
| cas3_cyano |
TIGR03158 |
CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short ... |
90-138 |
2.17e-04 |
|
CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family is a CRISPR-associated (Cas) family strictly associated with the Cyano subtype of CRISPR/Cas locus, found in several species of Cyanobacteria and several archaeal species. It contains helicase motifs and appears to represent the Cas3 protein of the Cyano subtype of CRISPR/Cas system.
Pssm-ID: 274457 [Multi-domain] Cd Length: 357 Bit Score: 43.35 E-value: 2.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 19113945 90 APTGSGKTIAYLFPILQklqlhvpGGYRAIIVAPTRELCEQIYRQAEKL 138
Cdd:TIGR03158 21 APTGAGKTLAWLTPLLH-------GENDTIALYPTNALIEDQTEAIKEF 62
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
290-378 |
2.84e-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: 40.62 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 290 RVVIFVQDIERAKALYTelLFDE--IHVGVIHGELPQAKRE-EALAKFRKGEIW--VLIATDLLARGIDFHGVKMVInfd 364
Cdd:cd18799 8 KTLIFCVSIEHAEFMAE--AFNEagIDAVALNSDYSDRERGdEALILLFFGELKppILVTVDLLTTGVDIPEVDNVV--- 82
|
90
....*....|....*..
gi 19113945 365 FPQSVHS---YIHRIGR 378
Cdd:cd18799 83 FLRPTESrtlFLQMLGR 99
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
89-148 |
3.28e-04 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 40.75 E-value: 3.28e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 89 CAPTGSGKTIaylfpILQKLQLHVPGGyRAIIVAPTRELCEQIYRQAEKLSFGTSLKIIE 148
Cdd:cd17926 24 VLPTGSGKTL-----TALALIAYLKEL-RTLIVVPTDALLDQWKERFEDFLGDSSIGLIG 77
|
|
| DEXHc_Brr2_1 |
cd18019 |
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ... |
72-145 |
5.56e-04 |
|
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: 41.20 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 72 IQRYAIPT-IGSKRDLLACAPTGSGKTIAYLFPILQKLQLHV-PGG------YRAIIVAPTRELCEQIYRqaeklSFGTS 143
Cdd:cd18019 21 IQSKLFPAaFETDENLLLCAPTGAGKTNVALLTILREIGKHRnPDGtinldaFKIVYIAPMKALVQEMVG-----NFSKR 95
|
..
gi 19113945 144 LK 145
Cdd:cd18019 96 LA 97
|
|
| PRK05580 |
PRK05580 |
primosome assembly protein PriA; Validated |
328-389 |
1.13e-03 |
|
primosome assembly protein PriA; Validated
Pssm-ID: 235514 [Multi-domain] Cd Length: 679 Bit Score: 41.68 E-value: 1.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113945 328 EEALAKFRKGEIWVLIATDLLARGIDFHGVKMV--INFDfpQSVHS------------YIHRIGRTGRAGNTGQAV 389
Cdd:PRK05580 470 EQLLAQFARGEADILIGTQMLAKGHDFPNVTLVgvLDAD--LGLFSpdfrasertfqlLTQVAGRAGRAEKPGEVL 543
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
70-246 |
1.21e-03 |
|
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: 40.09 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 70 TTIQRYAIPTIGSK--RDLLACAPTGSGKTIAYLFPILQklqlHVPGGYR---AIIVAPTRELCEQIYRQAEKLSFGTSL 144
Cdd:cd18047 25 SKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLS----QVEPANKypqCLCLSPTYELALQTGKVIEQMGKFYPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 145 KIIELSKSNEKIQEKapkLREKYDMCIGTPMRLVQ-AIQTGL-SFEKVEFFVMDEADRLFEP-GFIEQTDHILSACTSSn 221
Cdd:cd18047 101 LKLAYAVRGNKLERG---QKISEQIVIGTPGTVLDwCSKLKFiDPKKIKVFVLDEADVMIATqGHQDQSIRIQRMLPRN- 176
|
170 180
....*....|....*....|....*.
gi 19113945 222 iCKS-LFSATIPSRVEELAKVVTVDP 246
Cdd:cd18047 177 -CQMlLFSATFEDSVWKFAQKVVPDP 201
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
87-138 |
1.26e-03 |
|
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442728 [Multi-domain] Cd Length: 402 Bit Score: 41.12 E-value: 1.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 19113945 87 LACAPTGSGKTIAYLFPILQKLQlhvpGGYRAIIVAPTRELCEQIYRQAEKL 138
Cdd:COG3505 3 LVIGPTGSGKTVGLVIPNLTQLA----RGESVVVTDPKGDLAELTAGFRRRA 50
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
73-198 |
2.39e-03 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350773 [Multi-domain] Cd Length: 209 Bit Score: 39.27 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 73 QRYAIPTIGSKRDLLACAPTGSGKTIAYLFPILqklqlhVPGGYrAIIVAPTRELCEQIYRQAEKLsfGTSLKIIELSKS 152
Cdd:cd18015 23 QLETINATMAGRDVFLVMPTGGGKSLCYQLPAL------CSDGF-TLVVSPLISLMEDQLMALKKL--GISATMLNASSS 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 19113945 153 NEKIQEKAPKLREKYD---MCIGTPMRLVQ------AIQTGLSFEKVEFFVMDEA 198
Cdd:cd18015 94 KEHVKWVHAALTDKNSelkLLYVTPEKIAKskrfmsKLEKAYNAGRLARIAIDEV 148
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
315-383 |
2.86e-03 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 38.30 E-value: 2.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113945 315 VGVIHGELPQAKRE--EALakFRKGEIWVLIATDLLARGIDFH-------GVKMVINFDFPQ-SVHSYIHRIGRTGRAG 383
Cdd:cd18795 66 IAFHHAGLTREDRElvEEL--FREGLIKVLVATSTLAAGVNLPartviikGTQRYDGKGYRElSPLEYLQMIGRAGRPG 142
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
82-145 |
3.02e-03 |
|
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350778 [Multi-domain] Cd Length: 199 Bit Score: 38.95 E-value: 3.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113945 82 SKRDLLACAPTGSGKTIAYLFPILQKLQLHV-PGGY------RAIIVAPTRELCEQIyrqAEKlsFGTSLK 145
Cdd:cd18020 16 TNENMLICAPTGAGKTNIAMLTILHEIRQHVnQGGVikkddfKIVYIAPMKALAAEM---VEK--FSKRLA 81
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
73-198 |
4.40e-03 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 38.28 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 73 QRYAIPTIGSKRDLLACAPTGSGKTIAYLFP--ILQKLqlhvpggyrAIIVAPTRELCE-QIYRQAEKlsfGTSLKIIEL 149
Cdd:cd17920 17 QLEAINAVLAGRDVLVVMPTGGGKSLCYQLPalLLDGV---------TLVVSPLISLMQdQVDRLQQL---GIRAAALNS 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 19113945 150 SKSNEKIQEKAPKLRE-KYDMCIGTPMRLVQ-----AIQTGLSFEKVEFFVMDEA 198
Cdd:cd17920 85 TLSPEEKREVLLRIKNgQYKLLYVTPERLLSpdfleLLQRLPERKRLALIVVDEA 139
|
|
| Csf4_U |
cd09708 |
CRISPR/Cas system-associated DinG family helicase Csf4; CRISPR (Clustered Regularly ... |
83-138 |
4.52e-03 |
|
CRISPR/Cas system-associated DinG family helicase Csf4; 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; DinG family DNA helicase
Pssm-ID: 187839 [Multi-domain] Cd Length: 632 Bit Score: 39.57 E-value: 4.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 19113945 83 KRDLLACAPTGSGKTIAYLFPILQKLQLHvPGGyRAIIVAPTRELCEQIYRQAEKL 138
Cdd:cd09708 16 KRIGMLEASTGVGKTLAMIMAALTMLKER-PDQ-KIAIAVPTLALMGQLWSELERL 69
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
90-197 |
6.48e-03 |
|
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: 37.74 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113945 90 APTGSGKTIAYLFPILQKLQLHVpgGYRAIIVAPTRELC-EQIYRQAEKLSFGTSLKIIELSKSNekiqekAPKLRE--K 166
Cdd:cd18022 24 APTGSGKTIAAELAMFRAFNKYP--GSKVVYIAPLKALVrERVDDWKKRFEEKLGKKVVELTGDV------TPDMKAlaD 95
|
90 100 110
....*....|....*....|....*....|....
gi 19113945 167 YDMCIGTPMR---LVQAIQTGLSFEKVEFFVMDE 197
Cdd:cd18022 96 ADIIITTPEKwdgISRSWQTREYVQQVSLIIIDE 129
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
326-389 |
8.17e-03 |
|
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: 37.99 E-value: 8.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113945 326 KREEALAKFRKGEIWVLIATDLLARGIDFHGVKMV--------INF-DFPQSVHSY--IHRI-GRTGRAGNTGQAV 389
Cdd:cd18804 132 ALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgilnadsgLNSpDFRASERAFqlLTQVsGRAGRGDKPGKVI 207
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