|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
162-533 |
1.20e-118 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 358.31 E-value: 1.20e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 162 TFQQLdqeyKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQPANKGFRALIIS 241
Cdd:COG0513 3 SFADL----GLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQALILA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 242 PTRELASQIHRELIKISEGTGFRIHMIH-----KAAVAAKKFGPksskkfDILVTTPNRLIYLLKQDppGIDLASVEWLV 316
Cdd:COG0513 79 PTRELALQVAEELRKLAKYLGLRVATVYggvsiGRQIRALKRGV------DIVVATPGRLLDLIERG--ALDLSGVETLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 317 VDESDKLFEDGktgFRDQLASIfLACTSHKVRRAMFSATFAYDVEQWCKLNLDNVISVSIGARNSAVETVEQELLFVGSE 396
Cdd:COG0513 151 LDEADRMLDMG---FIEDIERI-LKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 397 TgKLLAVRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGI 476
Cdd:COG0513 227 D-KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGI 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400809 477 DFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDDKPLLRSVANVIQQ 533
Cdd:COG0513 306 DIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQ 362
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
176-377 |
7.14e-113 |
|
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: 335.33 E-value: 7.14e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQP-ANKGFRALIISPTRELASQIHREL 254
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPrKKKGLRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 255 IKISEGTGFRIHMIHKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLFEdgkTGFRDQ 334
Cdd:cd17957 81 LKLSKGTGLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGP--IDLSSVEYLVLDEADKLFE---PGFREQ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2203400809 335 LASIFLACTSHKVRRAMFSATFAYDVEQWCKLNLDNVISVSIG 377
Cdd:cd17957 156 TDEILAACTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
129-539 |
5.39e-79 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 258.95 E-value: 5.39e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 129 SGKLENLRKEKINFLRNKHKIHVQGTDLPDPIATFQQLdqeyKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLAS 208
Cdd:PLN00206 89 PGSTSGLSSSQAELLRRKLEIHVKGEAVPPPILSFSSC----GLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 209 APTGSGKTLAFSIPILMQLKQ------PANKGFRALIISPTRELASQIHRELIKISEGTGFRIHMIHKAAVAAKKFgPKS 282
Cdd:PLN00206 165 ADTGSGKTASFLVPIISRCCTirsghpSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQL-YRI 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 283 SKKFDILVTTPNRLIYLL-KQDppgIDLASVEWLVVDESDKLFEdgkTGFRDQLASIFLACTSHKVrrAMFSATFAYDVE 361
Cdd:PLN00206 244 QQGVELIVGTPGRLIDLLsKHD---IELDNVSVLVLDEVDCMLE---RGFRDQVMQIFQALSQPQV--LLFSATVSPEVE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 362 QWCKLNLDNVISVSIGARNSAVETVEQELLFVGSETGKLLAVRELVKKG-FNPPVLVFVQSIERAkELFHELI--YEGIN 438
Cdd:PLN00206 316 KFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSKQhFKPPAVVFVSSRLGA-DLLANAItvVTGLK 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 439 VDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTE 518
Cdd:PLN00206 395 ALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNE 474
|
410 420
....*....|....*....|.
gi 2203400809 519 DDKPLLRSVANVIQQAGCPVP 539
Cdd:PLN00206 475 EDRNLFPELVALLKSSGAAIP 495
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
134-539 |
4.95e-68 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 230.43 E-value: 4.95e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 134 NLRKEKINFLRNKHKIH-VQGTDLPDPIATFQqldqEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTG 212
Cdd:PTZ00110 102 ALSSKEVDEIRKEKEITiIAGENVPKPVVSFE----YTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 213 SGKTLAFSIPILMQLK-QPANK---GFRALIISPTRELASQIHRELIKIseGTGFRIHmiHKAAvaakkFG--PKSSKKF 286
Cdd:PTZ00110 178 SGKTLAFLLPAIVHINaQPLLRygdGPIVLVLAPTRELAEQIREQCNKF--GASSKIR--NTVA-----YGgvPKRGQIY 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 287 ------DILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLFEdgkTGFRDQLASIFlactsHKVR----RAMFSATF 356
Cdd:PTZ00110 249 alrrgvEILIACPGRLIDFLESNV--TNLRRVTYLVLDEADRMLD---MGFEPQIRKIV-----SQIRpdrqTLMWSATW 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 357 AYDVEQWCK-LNLDNVISVSIGARN-SAVETVEQELlFVGSETGKLLAVRELVKKGF--NPPVLVFVQSIERAKELFHEL 432
Cdd:PTZ00110 319 PKEVQSLARdLCKEEPVHVNVGSLDlTACHNIKQEV-FVVEEHEKRGKLKMLLQRIMrdGDKILIFVETKKGADFLTKEL 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 433 IYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKA 512
Cdd:PTZ00110 398 RLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGAS 477
|
410 420
....*....|....*....|....*..
gi 2203400809 513 ITFFTEDDKPLLRSVANVIQQAGCPVP 539
Cdd:PTZ00110 478 YTFLTPDKYRLARDLVKVLREAKQPVP 504
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
172-533 |
1.68e-64 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 218.52 E-value: 1.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 172 INSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL--KQPANKG---FRALIISPTREL 246
Cdd:PRK10590 8 LSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLitRQPHAKGrrpVRALILTPTREL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 247 ASQIHRELIKISEGTGFRiHMIHKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDppGIDLASVEWLVVDESDKLFEd 326
Cdd:PRK10590 88 AAQIGENVRDYSKYLNIR-SLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQN--AVKLDQVEILVLDEADRMLD- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 327 gkTGFRDQLASIfLACTSHKVRRAMFSATFAYDVEQWCKLNLDNVISVSIGARNSAVETVEQELLFVGSE-TGKLLAvrE 405
Cdd:PRK10590 164 --MGFIHDIRRV-LAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKrKRELLS--Q 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 406 LVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVI 485
Cdd:PRK10590 239 MIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVV 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2203400809 486 NYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDDKPLLRSVANVIQQ 533
Cdd:PRK10590 319 NYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKK 366
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
176-375 |
2.83e-63 |
|
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: 206.91 E-value: 2.83e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL---KQPANKGFRALIISPTRELASQIHR 252
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLlpePKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 253 ELIKISEGTGFRIHMIHkAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLFEDgktGFR 332
Cdd:cd00268 81 VARKLGKGTGLKVAAIY-GGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGK--LDLSNVKYLVLDEADRMLDM---GFE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2203400809 333 DQLASIFLACtSHKVRRAMFSATFAYDVEQWCKLNLDNVISVS 375
Cdd:cd00268 155 EDVEKILSAL-PKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
168-539 |
2.97e-63 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 215.93 E-value: 2.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 168 QEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQ--PANKGF----RALIIS 241
Cdd:PRK01297 90 HDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQtpPPKERYmgepRALIIA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 242 PTRELASQIHRELIKISEGTGFRIHMIHKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPPGIDLasVEWLVVDESD 321
Cdd:PRK01297 170 PTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARFCDILVATPGRLLDFNQRGEVHLDM--VEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 322 KLFEdgkTGFRDQLASIfLACTSHKVRRA--MFSATFAYDVEQWCKLNLDNVISVSIGARNSAVETVEQELLFV-GSETG 398
Cdd:PRK01297 248 RMLD---MGFIPQVRQI-IRQTPRKEERQtlLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVaGSDKY 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 399 KLLavRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDF 478
Cdd:PRK01297 324 KLL--YNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHI 401
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203400809 479 KGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDDKPLLRSVANVI-QQAGCPVP 539
Cdd:PRK01297 402 DGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLgRKISCEMP 463
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
162-599 |
4.29e-61 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 209.03 E-value: 4.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 162 TFQQLDqeykINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL-----KQPankGF- 235
Cdd:PRK11192 2 TFSELE----LDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfprRKS---GPp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 236 RALIISPTRELASQIHRELIKISEGTGFRIHMIhKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDppGIDLASVEWL 315
Cdd:PRK11192 75 RILILTPTRELAMQVADQARELAKHTHLDIATI-TGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEE--NFDCRAVETL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 316 VVDESDKLFEDGKTGFRDQLAsiflACTSHKVRRAMFSAT--------FAYDVeqwcklnLDNVISVSIGARNSAVETVE 387
Cdd:PRK11192 152 ILDEADRMLDMGFAQDIETIA----AETRWRKQTLLFSATlegdavqdFAERL-------LNDPVEVEAEPSRRERKKIH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 388 QELLFVGSETGKL-LAVREL----VKKGFnppvlVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGK 462
Cdd:PRK11192 221 QWYYRADDLEHKTaLLCHLLkqpeVTRSI-----VFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 463 IWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDDKPLLRSVANVIQQagcPV-PEY 541
Cdd:PRK11192 296 VNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEE---PLkARV 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400809 542 IKGFQKLLSKQKKKMIKKPlereSISTTPKCFLEKAKDKQKKvtgqnsKKKVALEDKS 599
Cdd:PRK11192 373 IDELRPKTKAPSEKKTGKP----SKKVLAKRAEKKEKEKEKP------KVKKRHRDTK 420
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
386-516 |
1.67e-55 |
|
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: 183.86 E-value: 1.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 386 VEQELLFVGSETGKLLAVRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWV 465
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2203400809 466 LICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFF 516
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
176-520 |
6.16e-55 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 193.09 E-value: 6.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLkQPANKGFRALIISPTRELASQIHREL- 254
Cdd:PRK11776 15 LLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL-DVKRFRVQALVLCPTRELADQVAKEIr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 255 --------IKI---SEGTGFRI------HMIHkaavaakkfgpksskkfdILVTTPNRLIYLLKQDppGIDLASVEWLVV 317
Cdd:PRK11776 94 rlarfipnIKVltlCGGVPMGPqidsleHGAH------------------IIVGTPGRILDHLRKG--TLDLDALNTLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 318 DESDKLFEdgkTGFRDQLASIFLACtsHKVRRAM-FSATFAYDVEQWCKLNLDNVISVSIGARNSAvETVEQELLFVgSE 396
Cdd:PRK11776 154 DEADRMLD---MGFQDAIDAIIRQA--PARRQTLlFSATYPEGIAAISQRFQRDPVEVKVESTHDL-PAIEQRFYEV-SP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 397 TGKLLAVRELVKKgFNP-PVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARG 475
Cdd:PRK11776 227 DERLPALQRLLLH-HQPeSCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARG 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2203400809 476 IDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDD 520
Cdd:PRK11776 306 LDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEE 350
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
154-518 |
1.40e-47 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 175.52 E-value: 1.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 154 TDLPDPIATFQQLDqeykINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL------ 227
Cdd:PRK04537 2 SDKPLTDLTFSSFD----LHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpal 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 228 --KQPANKgfRALIISPTRELASQIHRELIKISEGTGFRIHMIHkAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPP 305
Cdd:PRK04537 78 adRKPEDP--RALILAPTRELAIQIHKDAVKFGADLGLRFALVY-GGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 306 gIDLASVEWLVVDESDKLFEdgkTGFRDQLASIFLACTSHKVRRAM-FSATFAYDVEQWCKLNLDNVISVSIGARNSAVE 384
Cdd:PRK04537 155 -VSLHACEICVLDEADRMFD---LGFIKDIRFLLRRMPERGTRQTLlFSATLSHRVLELAYEHMNEPEKLVVETETITAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 385 TVEQELLFVGSETgKLLAVRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIW 464
Cdd:PRK04537 231 RVRQRIYFPADEE-KQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLE 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2203400809 465 VLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTE 518
Cdd:PRK04537 310 ILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACE 363
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
172-527 |
2.04e-46 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 173.11 E-value: 2.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 172 INSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKqPANKGFRALIISPTRELASQIH 251
Cdd:PRK11634 13 LKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD-PELKAPQILVLAPTRELAVQVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 252 RELikisegTGFRIHMIHKAAVA------------AKKFGPKsskkfdILVTTPNRLIYLLKQDPpgIDLASVEWLVVDE 319
Cdd:PRK11634 92 EAM------TDFSKHMRGVNVVAlyggqrydvqlrALRQGPQ------IVVGTPGRLLDHLKRGT--LDLSKLSGLVLDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 320 SDKLFedgKTGFRDQLASIfLACTSHKVRRAMFSATFAYDVEQWCKLNLDNVISVSIGARNSAVETVEQELLFVGSETGK 399
Cdd:PRK11634 158 ADEML---RMGFIEDVETI-MAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 400 LLAVRELVKKGFNPPVlVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFK 479
Cdd:PRK11634 234 EALVRFLEAEDFDAAI-IFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2203400809 480 GVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDDKPLLRSV 527
Cdd:PRK11634 313 RISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNI 360
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
171-529 |
2.58e-46 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 168.08 E-value: 2.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 171 KINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILmQLKQPANKGFRALIISPTRELASQI 250
Cdd:PTZ00424 34 KLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAAL-QLIDYDLNACQALILAPTRELAQQI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 251 HRELIKISEGTGFRIHMIHKAAVAAKKFGpKSSKKFDILVTTPNRLIYLLKQDPPGIDlaSVEWLVVDESDKLFEdgkTG 330
Cdd:PTZ00424 113 QKVVLALGDYLKVRCHACVGGTVVRDDIN-KLKAGVHMVVGTPGRVYDMIDKRHLRVD--DLKLFILDEADEMLS---RG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 331 FRDQLASIFLACTShKVRRAMFSATFAYDVEQWCKLNLDNVISVSIGARNSAVETVEQELLFVGSETGKLLAVRELVKKG 410
Cdd:PTZ00424 187 FKGQIYDVFKKLPP-DVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 411 FNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFP 490
Cdd:PTZ00424 266 TITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLP 345
|
330 340 350
....*....|....*....|....*....|....*....
gi 2203400809 491 TSSVEYIHRIGRTGRAGNKGKAITFFTEDDKPLLRSVAN 529
Cdd:PTZ00424 346 ASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIER 384
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
172-519 |
1.69e-45 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 166.30 E-value: 1.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 172 INSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAF-----------SIPILMQLKQPankgfRALII 240
Cdd:PRK04837 15 LHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFltatfhyllshPAPEDRKVNQP-----RALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 241 SPTRELASQIHRELIKISEGTGFrihmihKAAVAakkFGPKSSKK--------FDILVTTPNRLIYLLKQDPpgIDLASV 312
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGL------KLGLA---YGGDGYDKqlkvlesgVDILIGTTGRLIDYAKQNH--INLGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 313 EWLVVDESDKLFEdgkTGFRDQLASIFLACTSHKVRRAM-FSATFAYDVEQWCKLNLDNVISVSIGARNSAVETVEQELl 391
Cdd:PRK04837 159 QVVVLDEADRMFD---LGFIKDIRWLFRRMPPANQRLNMlFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEEL- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 392 FVGSETGKLLAVRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTAL 471
Cdd:PRK04837 235 FYPSNEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDV 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2203400809 472 LARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTED 519
Cdd:PRK04837 315 AARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEE 362
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
176-375 |
4.55e-45 |
|
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: 158.19 E-value: 4.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL--KQPANKGFRALIISPTRELASQIHRE 253
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyRPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 254 LIKISEGTGFRIHMI-----HKAAVAAKKFGPksskkfDILVTTPNRLIYLLKqDPPGIDLASVEWLVVDESDKLFEDgk 328
Cdd:cd17947 81 LQQLAQFTDITFALAvgglsLKAQEAALRARP------DIVIATPGRLIDHLR-NSPSFDLDSIEILVLDEADRMLEE-- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2203400809 329 tGFRDQLASIFLACtsHKVRRAM-FSATFAYDVEQWCKLNLDNVISVS 375
Cdd:cd17947 152 -GFADELKEILRLC--PRTRQTMlFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
162-355 |
9.22e-45 |
|
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: 157.85 E-value: 9.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 162 TFQQLDQEYKinsrLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQP-ANKGFRALII 240
Cdd:cd17959 2 GFQSMGLSPP----LLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHsPTVGARALIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 241 SPTRELASQIHRELIKISEGTGFRIHMIHKAAVAAKKFGPKSSKKfDILVTTPNRLIYLLKQDppGIDLASVEWLVVDES 320
Cdd:cd17959 78 SPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNP-DIIIATPGRLLHLLVEM--NLKLSSVEYVVFDEA 154
|
170 180 190
....*....|....*....|....*....|....*
gi 2203400809 321 DKLFEdgkTGFRDQLASIFLACTSHKvRRAMFSAT 355
Cdd:cd17959 155 DRLFE---MGFAEQLHEILSRLPENR-QTLLFSAT 185
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
189-362 |
2.54e-43 |
|
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: 152.40 E-value: 2.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 189 TPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQPaNKGFRALIISPTRELASQIHRELIKISEGTGFRIHMI 268
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKL-DNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 269 HKAAVAAKKFgpKSSKKFDILVTTPNRLIYLLKQDPpgiDLASVEWLVVDESDKLFEDgktGFRDQLASIfLACTSHKVR 348
Cdd:pfam00270 80 LGGDSRKEQL--EKLKGPDILVGTPGRLLDLLQERK---LLKNLKLLVLDEAHRLLDM---GFGPDLEEI-LRRLPKKRQ 150
|
170
....*....|....
gi 2203400809 349 RAMFSATFAYDVEQ 362
Cdd:pfam00270 151 ILLLSATLPRNLED 164
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
180-389 |
1.31e-42 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 151.88 E-value: 1.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 180 ILDAGFQMPTPIQMQAIPVMLHG-RELLASAPTGSGKTLAFSIPILMQLKQpaNKGFRALIISPTRELASQIHRELIKIS 258
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR--GKGGRVLVLVPTRELAEQWAEELKKLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 259 EGTGFRIHMIHKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLFEDgktGFRDQLASI 338
Cdd:smart00487 79 PSLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDK--LSLSNVDLVILDEAHRLLDG---GFGDQLEKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2203400809 339 fLACTSHKVRRAMFSATFAYDVEQWCKLNLDNVISVSIGarNSAVETVEQE 389
Cdd:smart00487 154 -LKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVG--FTPLEPIEQF 201
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
162-377 |
2.97e-42 |
|
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: 151.49 E-value: 2.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 162 TFQQLDqeykINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL---KQPANKGFR-- 236
Cdd:cd17967 1 SFEEAG----LRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledGPPSVGRGRrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 237 ----ALIISPTRELASQIHRELIKISEGTGFRI-------HMIHKAAvaakkfgpKSSKKFDILVTTPNRLIYLLKQDPp 305
Cdd:cd17967 77 aypsALILAPTRELAIQIYEEARKFSYRSGVRSvvvyggaDVVHQQL--------QLLRGCDILVATPGRLVDFIERGR- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203400809 306 gIDLASVEWLVVDESDKLFEdgkTGFRDQLASIFLACTSHKV--RR-AMFSATFAYDVEQWCKLNLDNVISVSIG 377
Cdd:cd17967 148 -ISLSSIKFLVLDEADRMLD---MGFEPQIRKIVEHPDMPPKgeRQtLMFSATFPREIQRLAADFLKNYIFLTVG 218
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
151-374 |
1.20e-39 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350711 [Multi-domain] Cd Length: 222 Bit Score: 144.44 E-value: 1.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 151 VQGTDLPDPIATFQQLDqeykINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLK-Q 229
Cdd:cd17953 2 VRGKDCPKPIQKWSQCG----LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKdQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 230 PANK---GFRALIISPTRELASQIHRELIKISEGTGFRIHMIHKAAVAAKKFGpKSSKKFDILVTTPNRLIYLLKQDPPG 306
Cdd:cd17953 78 RPVKpgeGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIA-ELKRGAEIVVCTPGRMIDILTANNGR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400809 307 I-DLASVEWLVVDESDKLFEdgkTGFRDQLASIFLACTSHKvRRAMFSATFAYDVEQWCKLNLDNVISV 374
Cdd:cd17953 157 VtNLRRVTYVVLDEADRMFD---MGFEPQIMKIVNNIRPDR-QTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
182-376 |
1.56e-36 |
|
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: 135.11 E-value: 1.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 182 DAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL---KQPANKGFRALIISPTRELASQIHRELIKIS 258
Cdd:cd17941 7 EAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLyreRWTPEDGLGALIISPTRELAMQIFEVLRKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 259 EGTGFRIHMIhkaaVAAKKFGPKSSK--KFDILVTTPNRLIYLLKQDpPGIDLASVEWLVVDESDKLFEdgkTGFRDQLA 336
Cdd:cd17941 87 KYHSFSAGLI----IGGKDVKEEKERinRMNILVCTPGRLLQHMDET-PGFDTSNLQMLVLDEADRILD---MGFKETLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2203400809 337 SIFLACTSHKvRRAMFSATFAYDVEQWCKLNLDNVISVSI 376
Cdd:cd17941 159 AIVENLPKSR-QTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
140-362 |
7.98e-36 |
|
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: 135.09 E-value: 7.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 140 INFLRNKH-KIHVQGTDLPDPIATFQqldqEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLA 218
Cdd:cd18052 21 INFDKYDEiPVEVTGRNPPPAILTFE----EANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 219 FSIPILMQLKQ-----PANKGFR---ALIISPTRELASQIHRELIKISEGTGFRihmihkaAVAAkkFGPKSS------- 283
Cdd:cd18052 97 FLLPVLTGMMKegltaSSFSEVQepqALIVAPTRELANQIFLEARKFSYGTCIR-------PVVV--YGGVSVghqirqi 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 284 -KKFDILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLFEdgkTGFRDQLASIFLAC-TSHKVRRA--MFSATFAYD 359
Cdd:cd18052 168 eKGCHILVATPGRLLDFIGRGK--ISLSKLKYLILDEADRMLD---MGFGPEIRKLVSEPgMPSKEDRQtlMFSATFPEE 242
|
...
gi 2203400809 360 VEQ 362
Cdd:cd18052 243 IQR 245
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
176-370 |
1.83e-35 |
|
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: 133.14 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPVML---------HGRELLASAPTGSGKTLAFSIPILMQLKQPANKGFRALIISPTREL 246
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLpsskstppyRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 247 ASQIHRELIKISEGTGFRIHMIHKAAVAAKK-------FGPKSSKKFDILVTTPNRLIYLLKQdPPGIDLASVEWLVVDE 319
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEqklllvdTSGRYLSRVDILVATPGRLVDHLNS-TPGFTLKHLRFLVIDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400809 320 SDKL----------------FEDGKTGFRDQLASIFLACTSHKVRRAMFSATFAYDVEQWCKLNLDN 370
Cdd:cd17956 160 ADRLlnqsfqdwletvmkalGRPTAPDLGSFGDANLLERSVRPLQKLLFSATLTRDPEKLSSLKLHR 226
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
176-367 |
7.31e-35 |
|
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: 131.59 E-value: 7.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPV-MLHGRELLASAPTGSGKTLAFSIPIL---MQLKQ-----PANKGFRALIISPTREL 246
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILerlLSQKSsngvgGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 247 ASQIHRELIKISEGTGFRIhMIHKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPPGID-LASVEWLVVDESDKLFE 325
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKI-ASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLAnLKSLRFLVLDEADRMLE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2203400809 326 DGKtgFRDqLASIFLA-----CTSHKVRRAM-FSATFAYDVEQWCKLN 367
Cdd:cd17946 160 KGH--FAE-LEKILELlnkdrAGKKRKRQTFvFSATLTLDHQLPLKLN 204
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
176-375 |
8.46e-35 |
|
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: 130.39 E-value: 8.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL----KQPANKGFRALIISPTRELASQIH 251
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkANLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 252 RELIKISEGTGFRIHMI-----HKAAVAAKKFgpkSSKKFDILVTTPNRLIYLLKQDPPGIDLASVEWLVVDESDKLFEd 326
Cdd:cd17960 81 EVLQSFLEHHLPKLKCQlliggTNVEEDVKKF---KRNGPNILVGTPGRLEELLSRKADKVKVKSLEVLVLDEADRLLD- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2203400809 327 gkTGFRDQLASIfLACTSHKVRRAMFSATFAYDVEQWCKLNLDNVISVS 375
Cdd:cd17960 157 --LGFEADLNRI-LSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
176-361 |
2.57e-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: 129.75 E-value: 2.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL-KQPA------NKGFRALIISPTRELAS 248
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYIsRLPPldeetkDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 249 QIHRELIKISEGTGFRIHMIhkaaVAAKKF---GPKSSKKFDILVTTPNRLIYLLkqDPPGIDLASVEWLVVDESDKLFE 325
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSI----VGGHSIeeqAFSLRNGCEILIATPGRLLDCL--ERRLLVLNQCTYVVLDEADRMID 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2203400809 326 dgkTGFRDQLASIF------------------LACTSHKVRRA-MFSATFAYDVE 361
Cdd:cd17945 155 ---MGFEPQVTKILdampvsnkkpdteeaeklAASGKHRYRQTmMFTATMPPAVE 206
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
398-507 |
2.83e-34 |
|
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: 125.79 E-value: 2.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 398 GKLLAVRELVKKGFNPPVLVFVQSIERAK-ELFHELiyEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGI 476
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEaELLLEK--EGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 2203400809 477 DFKGVNLVINYDFPTSSVEYIHRIGRTGRAG 507
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
176-375 |
3.48e-34 |
|
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: 128.44 E-value: 3.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL----KQPAnkgfrALIISPTRELASQIH 251
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCltehRNPS-----ALILTPTRELAVQIE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 252 RELIKISEGTgfrIHMIHKAAVAAKKFGP---KSSKKFDILVTTPNRLIYLLKQDppGIDLASVEWLVVDESDKLFedgK 328
Cdd:cd17962 76 DQAKELMKGL---PPMKTALLVGGLPLPPqlyRLQQGVKVIIATPGRLLDILKQS--SVELDNIKIVVVDEADTML---K 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2203400809 329 TGFRDQLASIFLAcTSHKVRRAMFSATFAYDVEQWCKLNLDNVISVS 375
Cdd:cd17962 148 MGFQQQVLDILEN-ISHDHQTILVSATIPRGIEQLAGQLLQNPVRIT 193
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
176-375 |
1.01e-33 |
|
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: 127.15 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL-KQPA---NKGFRALIISPTRELASQIH 251
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImDQRElekGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 252 RELIKISEGTGFRIHMIHKAA-----VAAKKFGPksskkfDILVTTPNRLIYLLKQDppGIDLASVEWLVVDESDKLFEd 326
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGskweqAKALQEGA------EIVVATPGRLIDMVKKK--ATNLQRVTYLVLDEADRMFD- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2203400809 327 gkTGFRDQLASIflactSHKVR----RAMFSATFAYDVEQWCKLNLDNVISVS 375
Cdd:cd17952 152 --MGFEYQVRSI-----VGHVRpdrqTLLFSATFKKKIEQLARDILSDPIRVV 197
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
172-374 |
3.89e-33 |
|
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: 125.77 E-value: 3.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 172 INSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPIL---MQLKQPANK--GFRALIISPTREL 246
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIqkiLKAKAESGEeqGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 247 ASQIHRELIKISEGTGFRIHMIHKAA-VAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPPgIDLASVEWLVVDESDKLFe 325
Cdd:cd17961 81 AQQVSKVLEQLTAYCRKDVRVVNLSAsSSDSVQRALLAEKPDIVVSTPARLLSHLESGSL-LLLSTLKYLVIDEADLVL- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2203400809 326 dgKTGFRDQLASIFLAcTSHKVRRAMFSATFAYDVEQWCKLNLDNVISV 374
Cdd:cd17961 159 --SYGYEEDLKSLLSY-LPKNYQTFLMSATLSEDVEALKKLVLHNPAIL 204
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
153-377 |
1.03e-32 |
|
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD box, X isoform, or DDX14) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. This protein has multiple conserved domains and is thought to play roles in both the nucleus and cytoplasm. Nuclear roles include transcriptional regulation, mRNP assembly, pre-mRNA splicing, and mRNA export. In the cytoplasm, this protein is thought to be involved in translation, cellular signaling, and viral replication. Misregulation of this gene has been implicated in tumorigenesis. Diseases associated with DDX3 include mental retardation, X-linked 102 and agenesis of the corpus callosum, with facial anomalies and robin sequence. DDX3 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350809 [Multi-domain] Cd Length: 249 Bit Score: 125.92 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 153 GTDLPDPIATFQQLDQEYKINSrllqNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL----- 227
Cdd:cd18051 13 GENCPPHIETFSDLDLGEIIRN----NIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIyeqgp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 228 -----KQPANKGFR-----ALIISPTRELASQIHRELIKISEGTGFRIHMIHKAAVAAKKFgpkssKKFD----ILVTTP 293
Cdd:cd18051 89 geslpSESGYYGRRkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQM-----RDLErgchLLVATP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 294 NRLIYLLKQDPPGIDlaSVEWLVVDESDKLFEdgkTGFRDQLASIFLACTSHK--VRRA-MFSATFAYDVEQWCKLNLDN 370
Cdd:cd18051 164 GRLVDMLERGKIGLD--YCKYLVLDEADRMLD---MGFEPQIRRIVEQDTMPPtgERQTlMFSATFPKEIQMLARDFLDN 238
|
....*..
gi 2203400809 371 VISVSIG 377
Cdd:cd18051 239 YIFLAVG 245
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
172-368 |
8.68e-32 |
|
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: 122.31 E-value: 8.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 172 INSRLLQNILDAGFQMPTPIQMQAIPVML-HGRELLASAPTGSGKTLAFSIP----ILMQLKQPANKGFRALIISPTREL 246
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPaiqsLLNTKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 247 ASQIHRELIKISEG-TGFRIHM------IHKAAVAAKKFGPksskkfDILVTTPNRLIYLLKQDPPGIDLASVEWLVVDE 319
Cdd:cd17964 81 ALQIAAEAKKLLQGlRKLRVQSavggtsRRAELNRLRRGRP------DILVATPGRLIDHLENPGVAKAFTDLDYLVLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2203400809 320 SDKLFEDgktGFRDQLASIfLACTSHKVRR----AMFSATFAYDVEQWCKLNL 368
Cdd:cd17964 155 ADRLLDM---GFRPDLEQI-LRHLPEKNADprqtLLFSATVPDEVQQIARLTL 203
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
162-375 |
3.36e-31 |
|
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: 120.50 E-value: 3.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 162 TFQQLDqeykINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQpANKGFRALIIS 241
Cdd:cd17954 1 TFKELG----VCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLE-NPQRFFALVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 242 PTRELASQIHRELIKISEGTGFR-------IHMIHKAAVAAKKfgPKsskkfdILVTTPNRLIYLLkQDPPGIDLASVEW 314
Cdd:cd17954 76 PTRELAQQISEQFEALGSSIGLKsavlvggMDMMAQAIALAKK--PH------VIVATPGRLVDHL-ENTKGFSLKSLKF 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400809 315 LVVDESDKLFEdgkTGFRDQLASIfLACTSHKVRRAMFSATFAYDVEQWCKLNLDNVISVS 375
Cdd:cd17954 147 LVMDEADRLLN---MDFEPEIDKI-LKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
168-360 |
3.77e-31 |
|
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: 120.10 E-value: 3.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 168 QEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLkQPANKGFRALIISPTRELA 247
Cdd:cd17940 2 EDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI-DPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 248 SQIHRELIKISEGTGFRIhMIHKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLFEDG 327
Cdd:cd17940 81 LQTSQVCKELGKHMGVKV-MVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGV--ADLSHCKTLVLDEADKLLSQD 157
|
170 180 190
....*....|....*....|....*....|...
gi 2203400809 328 KTGFRDQLasifLACTSHKVRRAMFSATFAYDV 360
Cdd:cd17940 158 FQPIIEKI----LNFLPKERQILLFSATFPLTV 186
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
168-355 |
5.09e-31 |
|
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: 120.02 E-value: 5.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 168 QEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQ-PAnkGFRALIISPTREL 246
Cdd:cd17955 2 EDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEdPY--GIFALVLTPTREL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 247 ASQIHRELIKISEGTGFR-------IHMIHKAAVAAKKfgPKsskkfdILVTTPNRLIYLLKQDPPGI-DLASVEWLVVD 318
Cdd:cd17955 80 AYQIAEQFRALGAPLGLRccvivggMDMVKQALELSKR--PH------IVVATPGRLADHLRSSDDTTkVLSRVKFLVLD 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 2203400809 319 ESDKLFEDgktGFRDQLASIFLACTSHKvRRAMFSAT 355
Cdd:cd17955 152 EADRLLTG---SFEDDLATILSALPPKR-QTLLFSAT 184
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
176-374 |
3.82e-29 |
|
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: 114.48 E-value: 3.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL-KQPANKGFR----ALIISPTRELASQI 250
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLdLQPIPREQRngpgVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 251 HRELIKISEgTGFRIHMIHKAAVAAKKFgPKSSKKFDILVTTPNRLIYLlkQDPPGIDLASVEWLVVDESDKLFEdgkTG 330
Cdd:cd17958 81 EAECSKYSY-KGLKSVCVYGGGNRNEQI-EDLSKGVDIIIATPGRLNDL--QMNNVINLKSITYLVLDEADRMLD---MG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2203400809 331 FRDQLASIFLACTSHKvRRAMFSATFAYDVEQWCKLNLDNVISV 374
Cdd:cd17958 154 FEPQIRKILLDIRPDR-QTIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
176-362 |
5.31e-28 |
|
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: 111.31 E-value: 5.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLK-QP---ANKGFRALIISPTRELASQIH 251
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINaQPpleRGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 252 RELIKISEGTGFRIHMIHKAAvaakkfgPKSSKKFD------ILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLFE 325
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGA-------PKGPQIRDlrrgveICIATPGRLIDFLDQGK--TNLRRVTYLVLDEADRMLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2203400809 326 dgkTGFRDQLASIFlactsHKVR----RAMFSATFAYDVEQ 362
Cdd:cd17966 152 ---MGFEPQIRKIV-----DQIRpdrqTLMWSATWPKEVRR 184
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
177-368 |
6.11e-28 |
|
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: 110.91 E-value: 6.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 177 LQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIP---ILMQLK-QPANkGFRALIISPTRELASQIH- 251
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPaieLLYKLKfKPRN-GTGVIIISPTRELALQIYg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 252 --RELIKISEGT-GFRIHMIHKAAVAAkkfgpKSSKKFDILVTTPNRLIYLLkQDPPGIDLASVEWLVVDESDKLFEdgk 328
Cdd:cd17942 81 vaKELLKYHSQTfGIVIGGANRKAEAE-----KLGKGVNILVATPGRLLDHL-QNTKGFLYKNLQCLIIDEADRILE--- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2203400809 329 TGFRDQLASIfLACTSHKVRRAMFSATFAYDVEQWCKLNL 368
Cdd:cd17942 152 IGFEEEMRQI-IKLLPKRRQTMLFSATQTRKVEDLARISL 190
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
176-364 |
1.23e-27 |
|
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: 110.49 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILmQLkqpankgFRALIISPTRELASQIHRELI 255
Cdd:cd17938 10 LIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-QI-------VVALILEPSRELAEQTYNCIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 256 KIS-EGTGFRI-HMIHKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLFEDGKTGFRD 333
Cdd:cd17938 82 NFKkYLDNPKLrVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGK--LDLSSVRFFVLDEADRLLSQGNLETIN 159
|
170 180 190
....*....|....*....|....*....|....
gi 2203400809 334 QLASIFLACTSHKVRRAM--FSATF-AYDVEQWC 364
Cdd:cd17938 160 RIYNRIPKITSDGKRLQVivCSATLhSFEVKKLA 193
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
426-507 |
3.80e-27 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 104.60 E-value: 3.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 426 KELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGR 505
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 2203400809 506 AG 507
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
168-365 |
6.37e-27 |
|
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350708 [Multi-domain] Cd Length: 208 Bit Score: 108.59 E-value: 6.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 168 QEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKqPANKGFRALIISPTRELA 247
Cdd:cd17950 5 RDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLE-PVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 248 SQIHRELIKISE-------GTGFRIHMIHKAAVAAKKFGPksskkfDILVTTPNRLIYLLKQDppGIDLASVEWLVVDES 320
Cdd:cd17950 84 FQISNEYERFSKympnvktAVFFGGVPIKKDIEVLKNKCP------HIVVGTPGRILALVREK--KLKLSHVKHFVLDEC 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2203400809 321 DKLFEDGKTgfRDQLASIFLACTSHKvRRAMFSATFAYDVEQWCK 365
Cdd:cd17950 156 DKMLEQLDM--RRDVQEIFRATPHDK-QVMMFSATLSKEIRPVCK 197
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
184-375 |
1.57e-26 |
|
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: 107.67 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 184 GFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLkQPA------NKGFRALIISPTRELASQIHRELIKI 257
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRL-LSLeprvdrSDGTLALVLVPTRELALQIYEVLEKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 258 segtGFRIHMIHKAAVAA--KKFGPKSS--KKFDILVTTPNRLIYLLkQDPPGIDLASVEWLVVDESDKLFEdgkTGFRD 333
Cdd:cd17949 89 ----LKPFHWIVPGYLIGgeKRKSEKARlrKGVNILIATPGRLLDHL-KNTQSFDVSNLRWLVLDEADRLLD---MGFEK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2203400809 334 QLASIFLACTSHKV------------RRAMFSATFAYDVEQWCKLNLDNVISVS 375
Cdd:cd17949 161 DITKILELLDDKRSkaggekskpsrrQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
176-373 |
5.85e-26 |
|
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: 105.04 E-value: 5.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKqPANKGFRALIISPTRELASQIHRELI 255
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLD-LERRHPQVLILAPTREIAVQIHDVFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 256 KISE-GTGFRIH-MIHKAAVAAKKfgpKSSKKFDILVTTPNRLIYLLKQDppGIDLASVEWLVVDESDKLFEDgktGFRD 333
Cdd:cd17943 80 KIGKkLEGLKCEvFIGGTPVKEDK---KKLKGCHIAVGTPGRIKQLIELG--ALNVSHVRLFVLDEADKLMEG---SFQK 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2203400809 334 QLASIFLACTSHKvRRAMFSATFAYdveqwcklNLDNVIS 373
Cdd:cd17943 152 DVNWIFSSLPKNK-QVIAFSATYPK--------NLDNLLA 182
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
131-377 |
5.69e-25 |
|
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: 104.71 E-value: 5.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 131 KLENLRKEKINFLRNKHKIHVQGTDLPDPIATFQQLDqeykINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAP 210
Cdd:cd18050 32 EVARMTQYDVEELRRKKEITIRGVGCPKPVFAFHQAN----FPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 211 TGSGKTLAFSIPILMQLK-QP---ANKGFRALIISPTRELASQIHRelIKISEGTGFRIHMIHKAAVAAKkfGPKS---S 283
Cdd:cd18050 108 TGSGKTLAYLLPAIVHINhQPyleRGDGPICLVLAPTRELAQQVQQ--VADDYGKSSRLKSTCIYGGAPK--GPQIrdlE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 284 KKFDILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLFEdgkTGFRDQLASIFLACTSHKvRRAMFSATFAYDVEQW 363
Cdd:cd18050 184 RGVEICIATPGRLIDFLEAGK--TNLRRCTYLVLDEADRMLD---MGFEPQIRKIVDQIRPDR-QTLMWSATWPKEVRQL 257
|
250
....*....|....
gi 2203400809 364 CKLNLDNVISVSIG 377
Cdd:cd18050 258 AEDFLRDYVQINIG 271
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
169-370 |
1.14e-24 |
|
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: 101.63 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 169 EYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQPANKgFRALIISPTRELAS 248
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRE-TQALVLAPTRELAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 249 QIHRELIKISEGTGFRIH-MIHKAAVAAKKFgpKSSKKFDILVTTPNRLIYLLKQDppGIDLASVEWLVVDESDKLFedg 327
Cdd:cd17939 80 QIQKVVKALGDYMGVKVHaCIGGTSVREDRR--KLQYGPHIVVGTPGRVFDMLQRR--SLRTDKIKMFVLDEADEML--- 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2203400809 328 KTGFRDQLASIFLACTShKVRRAMFSATFAYDVEQWCKLNLDN 370
Cdd:cd17939 153 SRGFKDQIYDIFQFLPP-ETQVVLFSATMPHEVLEVTKKFMRD 194
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
138-378 |
1.93e-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: 102.01 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 138 EKINFLRNKHKIHVQGTDLPDPIATFQqldqEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTL 217
Cdd:cd18049 1 QEVEQYRRSKEITVRGHNCPKPVLNFY----EANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 218 AFSIPILMQLK-QP---ANKGFRALIISPTRELASQIHRELIKISEGTGFRIHMIHKAAVAakkfGPKS---SKKFDILV 290
Cdd:cd18049 77 SYLLPAIVHINhQPfleRGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPK----GPQIrdlERGVEICI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 291 TTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLFEdgkTGFRDQLASIFLACTSHKvRRAMFSATFAYDVEQWCKLNLDN 370
Cdd:cd18049 153 ATPGRLIDFLEAGK--TNLRRCTYLVLDEADRMLD---MGFEPQIRKIVDQIRPDR-QTLMWSATWPKEVRQLAEDFLKD 226
|
....*...
gi 2203400809 371 VISVSIGA 378
Cdd:cd18049 227 YIHINIGA 234
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
176-375 |
2.83e-24 |
|
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: 101.67 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQ-LKQPANKGF-----RALIISPTRELASQ 249
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRlLRYKLLAEGpfnapRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 250 IHRELIKISEGTGFRIHMIH----KAAVAAKKFGpksskKFDILVTTPNRLIYLLKQdppGI-DLASVEWLVVDESDKLF 324
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITggrtKRQIRNPHFE-----EVDILVATPGALSKLLTS---RIySLEQLRHLVLDEADTLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2203400809 325 EDgktGFRDQLASIFLACTSHKVRRA------------MFSATFAYDVEQWcklnLDNVISVS 375
Cdd:cd17948 153 DD---SFNEKLSHFLRRFPLASRRSEntdgldpgtqlvLVSATMPSGVGEV----LSKVIDVD 208
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
172-361 |
3.24e-24 |
|
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: 100.34 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 172 INSRLLQNILDAGFQMPTPIQMQAIPVMLHG--RELLASAPTGSGKTLAFSIPILMQLkQPANKGFRALIISPTRELASQ 249
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-DPTLKSPQALCLAPTRELARQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 250 IHRELIKISEGTGFRIHmihkAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDppGIDLASVEWLVVDESDKLFEDGkt 329
Cdd:cd17963 80 IGEVVEKMGKFTGVKVA----LAVPGNDVPRGKKITAQIVIGTPGTVLDWLKKR--QLDLKKIKILVLDEADVMLDTQ-- 151
|
170 180 190
....*....|....*....|....*....|....
gi 2203400809 330 GFRDQLASI--FLactSHKVRRAMFSATFAYDVE 361
Cdd:cd17963 152 GHGDQSIRIkrML---PRNCQILLFSATFPDSVR 182
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
176-355 |
4.33e-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: 100.49 E-value: 4.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILM-----QLKQP--ANKGFRALIISPTRELAS 248
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMfaleqEKKLPfiKGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 249 QIHrELI-----KISEGTGFRIH---------MIHKAAVAakkfgpksSKKFDILVTTPNRLIYLLKQDPpgIDLASVEW 314
Cdd:cd17951 81 QTH-EVIeyyckALQEGGYPQLRcllciggmsVKEQLEVI--------RKGVHIVVATPGRLMDMLNKKK--INLDICRY 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2203400809 315 LVVDESDKLFEdgkTGFRDQLASIFLACTSHKvRRAMFSAT 355
Cdd:cd17951 150 LCLDEADRMID---MGFEEDIRTIFSYFKGQR-QTLLFSAT 186
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
201-529 |
9.07e-23 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 102.41 E-value: 9.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 201 HGRELLASAPTGSGKTLAFSIpILMQLKQPAnkgfRALIISPTRELASQIHRELIKISEGTGFrihmihkaavaakkFGP 280
Cdd:COG1061 99 GGGRGLVVAPTGTGKTVLALA-LAAELLRGK----RVLVLVPRRELLEQWAEELRRFLGDPLA--------------GGG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 281 KSSKKFDILVTTPNRLIYLLKQD--PPGIDLasvewLVVDE----SDKLFEdgktgfrdQLASIFlactsHKVRRAMFSA 354
Cdd:COG1061 160 KKDSDAPITVATYQSLARRAHLDelGDRFGL-----VIIDEahhaGAPSYR--------RILEAF-----PAAYRLGLTA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 355 T-FAYDVEQWCKLNLDNV----------------------ISVSIGARNSAVETVEQEL--LFVGSETGKLLAVRELVKK 409
Cdd:COG1061 222 TpFRSDGREILLFLFDGIvyeyslkeaiedgylappeyygIRVDLTDERAEYDALSERLreALAADAERKDKILRELLRE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 410 -GFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYD 488
Cdd:COG1061 302 hPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2203400809 489 fPTSS-VEYIHRIGRTGR-AGNKGKAITF-FTEDDKPLLRSVAN 529
Cdd:COG1061 382 -PTGSpREFIQRLGRGLRpAPGKEDALVYdFVGNDVPVLEELAK 424
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
188-326 |
2.17e-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: 93.60 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 188 PTPIQMQAIPVMLHGR----------------ELLASAPTGSGKTLAFSIPILMQLKQ----------------PANKGF 235
Cdd:cd17965 31 PSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKRqeqepfeeaeeeyesaKDTGRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 236 RALIISPTRELASQIHRELIKISEGTGFRIHMI-HKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPPgiDLASVEW 314
Cdd:cd17965 111 RSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFsSGFGPSYQRLQLAFKGRIDILVTTPGKLASLAKSRPK--ILSRVTH 188
|
170
....*....|..
gi 2203400809 315 LVVDESDKLFED 326
Cdd:cd17965 189 LVVDEADTLFDR 200
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
176-360 |
1.96e-20 |
|
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: 89.81 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLkQPANKGFRALIISPTRELASQIHRELI 255
Cdd:cd18046 10 LLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI-DTSLKATQALVLAPTRELAQQIQKVVM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 256 KISEGTGFRIHM-IHKAAVAAKKFGPKSSKKfdILVTTPNRLIYLLKQDppGIDLASVEWLVVDESDKLFEdgkTGFRDQ 334
Cdd:cd18046 89 ALGDYMGIKCHAcIGGTSVRDDAQKLQAGPH--IVVGTPGRVFDMINRR--YLRTDYIKMFVLDEADEMLS---RGFKDQ 161
|
170 180
....*....|....*....|....*.
gi 2203400809 335 LASIFLACTShKVRRAMFSATFAYDV 360
Cdd:cd18046 162 IYDIFQKLPP-DTQVVLLSATMPNDV 186
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
188-513 |
5.78e-19 |
|
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box helicases found associated with a bacterial ATP-dependent DNA ligase, part of a four-gene system that occurs in about 12 % of prokaryotic reference genomes. The actual motif in this family is DE[VILW]H.
Pssm-ID: 274994 [Multi-domain] Cd Length: 804 Bit Score: 91.07 E-value: 5.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 188 PTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL---KQPANKGFRALIISPTRELASQIHRELIKISEGTG-- 262
Cdd:TIGR04121 14 PRPFQLEMWAAALEGRSGLLIAPTGSGKTLAGFLPSLIDLagpEAPKEKGLHTLYITPLRALAVDIARNLQAPIEELGlp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 263 FRIHM------IHKAAvAAKKFGPksskkfDILVTTPNRLIYLLKQ-DPPGI--DLASVewlVVDESDKLFEdGKTGFRD 333
Cdd:TIGR04121 94 IRVETrtgdtsSSERA-RQRKKPP------DILLTTPESLALLLSYpDAARLfkDLRCV---VVDEWHELAG-SKRGDQL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 334 QLASIFLACTSHKVRRAMFSATFAyDVEQ---WCkLNLDNVISVSIGA---RNSAVETV--EQELLFVGSETGKLLAVRE 405
Cdd:TIGR04121 163 ELALARLRRLAPGLRRWGLSATIG-NLEEarrVL-LGVGGAPAVLVRGklpKAIEVISLlpESEERFPWAGHLGLRALPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 406 LVKK-GFNPPVLVFVQSIERAKELFHELIYegINVD---VI---HAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDF 478
Cdd:TIGR04121 241 VYAEiDQARTTLVFTNTRSQAELWFQALWE--ANPEfalPIalhHGSLDREQRRWVEAAMAAGRLRAVVCTSSLDLGVDF 318
|
330 340 350
....*....|....*....|....*....|....*.
gi 2203400809 479 KGVNLVINYDFPTSSVEYIHRIGRTG-RAGNKGKAI 513
Cdd:TIGR04121 319 GPVDLVIQIGSPKGVARLLQRAGRSNhRPGEPSRAL 354
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
189-507 |
1.13e-18 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 89.57 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 189 TPIQMQAIP-VMLHGRELLASAPTGSGKTLAFSIPILMQLkqpaNKGFRALIISPTRELASQIHRELIKISEGTGFRIhm 267
Cdd:COG1204 24 YPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKAL----LNGGKALYIVPLRALASEKYREFKRDFEELGIKV-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 268 ihKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPPGIDlaSVEWLVVDESDKLfEDGKTGFRDQLAsifLACTSHKV 347
Cdd:COG1204 98 --GVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPSWLR--DVDLVVVDEAHLI-DDESRGPTLEVL---LARLRRLN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 348 RRAMF---SATF--AYDVEQWckLNLDNVisvsigarNSAVETVEQELLFV---------GSETGK---LLAVRELVKKG 410
Cdd:COG1204 170 PEAQIvalSATIgnAEEIAEW--LDAELV--------KSDWRPVPLNEGVLydgvlrfddGSRRSKdptLALALDLLEEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 411 fnPPVLVFVQSI-----------------------ERAKELFHELIYEGINVDVI--------------HAERTQQQRDN 453
Cdd:COG1204 240 --GQVLVFVSSRrdaeslakkladelkrrltpeerEELEELAEELLEVSEETHTNekladclekgvafhHAGLPSELRRL 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400809 454 TVHSFRAGKIWVLICTALLArgidfKGVNL----VI--------NYDFPTSsvEYIHRIGRTGRAG 507
Cdd:COG1204 318 VEDAFREGLIKVLVATPTLA-----AGVNLparrVIirdtkrggMVPIPVL--EFKQMAGRAGRPG 376
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
176-360 |
2.55e-18 |
|
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: 83.67 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 176 LLQNILDAGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILmQLKQPANKGFRALIISPTRELASQIHRELI 255
Cdd:cd18045 10 LLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVL-QCLDIQVRETQALILSPTRELAVQIQKVLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 256 KISEGTGFRIHmihkAAVAAKKFGPKSSK---KFDILVTTPNRLIYLLKQDppGIDLASVEWLVVDESDKLFEDgktGFR 332
Cdd:cd18045 89 ALGDYMNVQCH----ACIGGTSVGDDIRKldyGQHIVSGTPGRVFDMIRRR--SLRTRHIKMLVLDEADEMLNK---GFK 159
|
170 180 190
....*....|....*....|....*....|
gi 2203400809 333 DQLASIF--LACTSHKVrraMFSATFAYDV 360
Cdd:cd18045 160 EQIYDVYryLPPATQVV---LVSATLPQDI 186
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
202-319 |
1.68e-17 |
|
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: 80.32 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 202 GRELLASAPTGSGKTLAFSIPILMQLKQPANKGFRALIISPTRELASQIHRELIKISEGTGFRIHMIHKAAVAAKKFGPK 281
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLEIPVAVRHGDTSQSEKAK 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 2203400809 282 SSKKF-DILVTTPNRLIYLLKQDPPGIDLASVEWLVVDE 319
Cdd:cd17922 81 QLKNPpGILITTPESLELLLVNKKLRELFAGLRYVVVDE 119
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
185-504 |
2.45e-17 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 85.92 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 185 FQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL-----KQPANKGFRALIISPTRELASQIHRELIK--- 256
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDELarrprPGELPDGLRVLYISPLKALANDIERNLRAple 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 257 -ISEGTGFRIHMIhKAAV------AAKKfgpkssKKF-----DILVTTPNRLiYLLKQDPPGID-LASVEWLVVDE---- 319
Cdd:COG1201 102 eIGEAAGLPLPEI-RVGVrtgdtpASER------QRQrrrppHILITTPESL-ALLLTSPDARElLRGVRTVIVDEihal 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 320 -SDKlfedgktgfR-DQLAsifL------ACTSHKVRRAMFSATFA-----------YDVEQWCKlnldnVISVSIGAR- 379
Cdd:COG1201 174 aGSK---------RgVHLA---LslerlrALAPRPLQRIGLSATVGpleevarflvgYEDPRPVT-----IVDAGAGKKp 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 380 ----NSAVETVEQELLFVGSETGKLLA-VRELVKKgfNPPVLVFV----QSiERakeLFHEL--IYEGINVDV-IH---- 443
Cdd:COG1201 237 dlevLVPVEDLIERFPWAGHLWPHLYPrVLDLIEA--HRTTLVFTntrsQA-ER---LFQRLneLNPEDALPIaAHhgsl 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203400809 444 -AErtqqQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTG 504
Cdd:COG1201 311 sRE----QRLEVEEALKAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAG 368
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
189-373 |
7.93e-15 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 72.68 E-value: 7.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 189 TPIQMQAI-PVMLHGRELLASAPTGSGKTLAFSIPILMQLKQpanKGFRALIISPTRELASQIHRELIKISEGTGFRIHM 267
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALAT---SGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 268 IhkaaVAAKKFGPKSSKKFDILVTTPNRL-IYLLKqdPPGIDLASVEWLVVDESdKLFEDGKTGFRDQLASIFLACTSHK 346
Cdd:cd17921 80 L----TGDPSVNKLLLAEADILVATPEKLdLLLRN--GGERLIQDVRLVVVDEA-HLIGDGERGVVLELLLSRLLRINKN 152
|
170 180
....*....|....*....|....*....
gi 2203400809 347 VRRAMFSATF--AYDVEQWckLNLDNVIS 373
Cdd:cd17921 153 ARFVGLSATLpnAEDLAEW--LGVEDLIR 179
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
192-523 |
2.01e-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: 76.41 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 192 QMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQpaNKGFRALIISPTRELASQIHRELIKISEGTGFRIHmihka 271
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE--DPGATALYLYPTKALARDQLRRLRELAEALGLGVR----- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 272 avAAKKFG--PKSSKKF-----DILVTTPNRLIY-LLKQDPPGID-LASVEWLVVDES---DKLFedgktG------FR- 332
Cdd:COG1205 134 --VATYDGdtPPEERRWirehpDIVLTNPDMLHYgLLPHHTRWARfFRNLRYVVIDEAhtyRGVF-----GshvanvLRr 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 333 -----DQLAS--IFLACtshkvrramfSATFAYDVEQWCKL-NLD-NVISVSiGARNSavetvEQELLFV---------- 393
Cdd:COG1205 207 lrricRHYGSdpQFILA----------SATIGNPAEHAERLtGRPvTVVDED-GSPRG-----ERTFVLWnpplvddgir 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 394 ---GSETGKLLAvrELVKKGFNppVLVFVQSI-------ERAKELFHELIYeGINVDVIHAERTQQQRDNTVHSFRAGKI 463
Cdd:COG1205 271 rsaLAEAARLLA--DLVREGLR--TLVFTRSRrgaellaRYARRALREPDL-ADRVAAYRAGYLPEERREIERGLRSGEL 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203400809 464 WVLICT-AL-LarGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDdkPL 523
Cdd:COG1205 346 LGVVSTnALeL--GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVAGDD--PL 403
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
190-360 |
2.19e-14 |
|
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: 72.19 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 190 PIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLK---QPANKGF--RALIISPTRELASQIHRELIKISEgtgfr 264
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQedqQPRKRGRapKVLVLAPTRELANQVTKDFKDITR----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 265 ihmihKAAVAAKKFGPKSSKKF-------DILVTTPNRLIYLLKQDPpgIDLASVEWLVVDESDKLFEdgkTGFRDQLAS 337
Cdd:cd17944 90 -----KLSVACFYGGTPYQQQIfairngiDILVGTPGRIKDHLQNGR--LDLTKLKHVVLDEVDQMLD---MGFAEQVEE 159
|
170 180 190
....*....|....*....|....*....|
gi 2203400809 338 I----FLACTSHKVRRAMFSAT---FAYDV 360
Cdd:cd17944 160 IlsvsYKKDSEDNPQTLLFSATcpdWVYNV 189
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
202-355 |
3.78e-14 |
|
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: 69.74 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 202 GRELLASAPTGSGKTLAFSIPILMQLKQpanKGFRALIISPTRELASQIHRELIKISeGTGFRIHMIHkaavAAKKFGPK 281
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLK---KGKKVLVLVPTKALALQTAERLRELF-GPGIRVAVLV----GGSSAEER 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400809 282 SSKKF---DILVTTPNRlIYLLKQDPPGIDLASVEWLVVDESDKLfeDGKTGFRDQLASIFLACTSHKVRRAMFSAT 355
Cdd:cd00046 73 EKNKLgdaDIIIATPDM-LLNLLLREDRLFLKDLKLIIVDEAHAL--LIDSRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
147-356 |
4.94e-14 |
|
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: 71.98 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 147 HKIHVQGTDLPDPIATFQQLdQEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHG--RELLASAPTGSGKTLAFSIPIL 224
Cdd:cd18048 1 HRVEVLQRDPTSPLFSVKSF-EELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAML 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 225 MQLKqpANKGF-RALIISPTRELASQIHR---ELIKISEGtgfrIHMIHkaAVAAKKFGPKSSKKFDILVTTPNRLI--- 297
Cdd:cd18048 80 SRVD--ALKLYpQCLCLSPTFELALQTGKvveEMGKFCVG----IQVIY--AIRGNRPGKGTDIEAQIVIGTPGTVLdwc 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400809 298 YLLKQdppgIDLASVEWLVVDESDKLFEdgKTGFRDQlasiflactSHKVRRAM--------FSATF 356
Cdd:cd18048 152 FKLRL----IDVTNISVFVLDEADVMIN--VQGHSDH---------SVRVKRSMpkecqmllFSATF 203
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
399-519 |
1.35e-13 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 74.00 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 399 KLLAVRELVKK--GFNPP--VLVFVQSIERAKELFHELIYEGINVD--VIHAER------TQQQRDNTVHSFRAGKIWVL 466
Cdd:COG1111 336 KLSKLREILKEqlGTNPDsrIIVFTQYRDTAEMIVEFLSEPGIKAGrfVGQASKegdkglTQKEQIEILERFRAGEFNVL 415
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2203400809 467 ICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRaGNKGKAITFFTED 519
Cdd:COG1111 416 VATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGR-KREGRVVVLIAKG 467
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
192-507 |
1.23e-12 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 70.68 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 192 QMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKqpanKGFRALIISPTRELASQIHRELIKISEgTGFRIHMihka 271
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFL----AGLKSIYIVPLRSLAMEKYEELSRLRS-LGMRVKI---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 272 AVAAKKFGPKSSKKFDILVTTPNRLIYLLKQDPPGIDlaSVEWLVVDESDKLFEDGKTGFRDQLASIfLACTSHKVRRAM 351
Cdd:PRK01172 98 SIGDYDDPPDFIKRYDVVILTSEKADSLIHHDPYIIN--DVGLIVADEIHIIGDEDRGPTLETVLSS-ARYVNPDARILA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 352 FSATF--AYDVEQWckLNLDNVISvsiGARNSAVET---VEQELLFVGSETGKL---LAVRELVKKGFNppVLVFVQSIE 423
Cdd:PRK01172 175 LSATVsnANELAQW--LNASLIKS---NFRPVPLKLgilYRKRLILDGYERSQVdinSLIKETVNDGGQ--VLVFVSSRK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 424 RAK---------------------------ELFHELIYEGINVDviHAERTQQQRDNTVHSFRAGKIWVLICTALLARGI 476
Cdd:PRK01172 248 NAEdyaemliqhfpefndfkvssennnvydDSLNEMLPHGVAFH--HAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGV 325
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2203400809 477 DFKGvNLVINYDF---------PTSSVEYIHRIGRTGRAG 507
Cdd:PRK01172 326 NLPA-RLVIVRDItrygnggirYLSNMEIKQMIGRAGRPG 364
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
414-517 |
8.36e-12 |
|
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: 61.18 E-value: 8.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 414 PVLVFVQSIERAKELFHELIyeginvdvihaertqqqrdntvhsfragkiwVLICTALLARGIDFKGVNLVINYDFPTSS 493
Cdd:cd18785 5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSA 53
|
90 100
....*....|....*....|....
gi 2203400809 494 VEYIHRIGRTGRAGNKGKAITFFT 517
Cdd:cd18785 54 ASYIQRVGRAGRGGKDEGEVILFV 77
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
192-319 |
1.26e-11 |
|
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: 63.76 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 192 QMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQpaNKGFRALIISPTRELA-SQIhRELIKISEGTGFRIHMihk 270
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLR--DPGSRALYLYPTKALAqDQL-RSLRELLEQLGLGIRV--- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400809 271 AAVAAKKfgPKSSKKF------DILVTTPNRLIYLLkqDPPGID----LASVEWLVVDE 319
Cdd:cd17923 79 ATYDGDT--PREERRAiirnppRILLTNPDMLHYAL--LPHHDRwarfLRNLRYVVLDE 133
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
168-356 |
3.45e-11 |
|
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: 62.82 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 168 QEYKINSRLLQNILDAGFQMPTPIQMQAIPVMLHG--RELLASAPTGSGKTLAFSIPILMQLkQPANKGFRALIISPTRE 245
Cdd:cd18047 4 EELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV-EPANKYPQCLCLSPTYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 246 LASQIHRELIKISEgtgFRIHMIHKAAVAAKKFGPKSSKKFDILVTTPNRLI-YLLKQDPpgIDLASVEWLVVDESDKLF 324
Cdd:cd18047 83 LALQTGKVIEQMGK---FYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLdWCSKLKF--IDPKKIKVFVLDEADVMI 157
|
170 180 190
....*....|....*....|....*....|..
gi 2203400809 325 edGKTGFRDQLASIfLACTSHKVRRAMFSATF 356
Cdd:cd18047 158 --ATQGHQDQSIRI-QRMLPRNCQMLLFSATF 186
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
190-319 |
3.79e-11 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 61.97 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 190 PIQMQAI-PVMLHGRELLASAPTGSGKTLafsIPILMQLKQpANKGFRALIISPTRELASQIHRELiKISEGTGFRIhmi 268
Cdd:cd18028 4 PPQAEAVrAGLLKGENLLISIPTASGKTL---IAEMAMVNT-LLEGGKALYLVPLRALASEKYEEF-KKLEEIGLKV--- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2203400809 269 hkaAVAAKKF--GPKSSKKFDILVTTPNRLIYLLKQDPPGIDLASVewLVVDE 319
Cdd:cd18028 76 ---GISTGDYdeDDEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGV--VVVDE 123
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
189-319 |
5.10e-11 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 65.68 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 189 TPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQPANKG-----FRALIISPTRELASQIHRELI-------K 256
Cdd:PRK13767 34 TPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFRLGREGeledkVYCLYVSPLRALNNDIHRNLEeplteirE 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400809 257 ISEGTGFRIHMIhKAAVaakKFGPKSS--------KKFDILVTTPNRLIYLL-----KQDppgidLASVEWLVVDE 319
Cdd:PRK13767 114 IAKERGEELPEI-RVAI---RTGDTSSyekqkmlkKPPHILITTPESLAILLnspkfREK-----LRTVKWVIVDE 180
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
389-516 |
2.06e-10 |
|
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: 58.76 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 389 ELLFVGSETGKLLAVRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLIC 468
Cdd:cd18794 7 SVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVA 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2203400809 469 TALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFF 516
Cdd:cd18794 87 TVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
399-513 |
3.56e-10 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 58.52 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 399 KLLAVRELVKKGF-------NPPVLVFVQSIERAKELFHELIYEGINVDVI----HAER------TQQQRDNTVHSFRAG 461
Cdd:cd18801 10 KLEKLEEIVKEHFkkkqegsDTRVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASGksskgmSQKEQKEVIEQFRKG 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2203400809 462 KIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRaGNKGKAI 513
Cdd:cd18801 90 GYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVV 140
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
399-519 |
9.35e-10 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 61.43 E-value: 9.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 399 KLLAVRELVKK--GFNPP--VLVFVQSIERAKELFHELIYEGINvdvihAER-------------TQQQRDNTVHSFRAG 461
Cdd:PRK13766 348 KLEKLREIVKEqlGKNPDsrIIVFTQYRDTAEKIVDLLEKEGIK-----AVRfvgqaskdgdkgmSQKEQIEILDKFRAG 422
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400809 462 KIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRaGNKGKAITFFTED 519
Cdd:PRK13766 423 EFNVLVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRTGR-QEEGRVVVLIAKG 479
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
399-505 |
2.05e-09 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 59.89 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 399 KLLA-VRELVKKGFnpPVLVFVQSIERAKELFHEL--IYEGINVDVIHAErtQQQRDNTVHSFRAGKIWVLICTALLARG 475
Cdd:COG4098 307 KLLKwLKKRLKEGR--QLLIFVPTIELLEQLVALLqkLFPEERIAGVHAE--DPERKEKVQAFRDGEIPILVTTTILERG 382
|
90 100 110
....*....|....*....|....*....|....
gi 2203400809 476 IDFKGVN-LVINYD---FPTSSVEYIHriGRTGR 505
Cdd:COG4098 383 VTFPNVDvAVLGADhpvFTEAALVQIA--GRVGR 414
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
192-525 |
2.66e-09 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 59.77 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 192 QMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQlkqpanKGfRALIISPtreLAS----QIhRELikisEGTGFRIHM 267
Cdd:COG0514 22 QEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLL------PG-LTLVVSP---LIAlmkdQV-DAL----RAAGIRAAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 268 IH-----------KAAVAAKKFgpksskkfDILVTTPNRL-----IYLLKQDPpgIDLasvewLVVDE----SD------ 321
Cdd:COG0514 87 LNsslsaeerrevLRALRAGEL--------KLLYVAPERLlnprfLELLRRLK--ISL-----FAIDEahciSQwghdfr 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 322 ----KLFEdgktgFRDQLASI-FLACT---SHKVRRamfsatfayDVEQwcKLNLDNViSVSIG--ARNS---AVETVEQ 388
Cdd:COG0514 152 pdyrRLGE-----LRERLPNVpVLALTataTPRVRA---------DIAE--QLGLEDP-RVFVGsfDRPNlrlEVVPKPP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 389 EllfvgsetGKLLAVRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLIC 468
Cdd:COG0514 215 D--------DKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVA 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400809 469 TALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDDKPLLR 525
Cdd:COG0514 287 TIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQR 343
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
419-523 |
5.51e-09 |
|
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: 55.04 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 419 VQSIERAKELFHELIYEgINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIH 498
Cdd:cd18810 35 IESIEKLATQLRQLVPE-ARIAIAHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLY 113
|
90 100
....*....|....*....|....*.
gi 2203400809 499 RI-GRTGRAGNKGKAItFFTEDDKPL 523
Cdd:cd18810 114 QLrGRVGRSKERAYAY-FLYPDQKKL 138
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
396-503 |
2.67e-08 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 56.77 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 396 ETGKLLAVRELVKKGFNP--PVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGK-IWV-LICTAL 471
Cdd:COG0553 531 RSAKLEALLELLEELLAEgeKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVfLISLKA 610
|
90 100 110
....*....|....*....|....*....|....*...
gi 2203400809 472 LARGIDFKGVNLVINYDFP-TSSVEY-----IHRIGRT 503
Cdd:COG0553 611 GGEGLNLTAADHVIHYDLWwNPAVEEqaidrAHRIGQT 648
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
398-501 |
3.01e-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: 52.48 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 398 GKLLAVRELVKKGFNPP--VLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAG-KIWV-LICTALLA 473
Cdd:cd18793 11 GKLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVfLLSTKAGG 90
|
90 100 110
....*....|....*....|....*....|....
gi 2203400809 474 RGIDFKGVNLVINYDFP-TSSVEY-----IHRIG 501
Cdd:cd18793 91 VGLNLTAANRVILYDPWwNPAVEEqaidrAHRIG 124
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
445-509 |
5.11e-08 |
|
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: 52.21 E-value: 5.11e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203400809 445 ERTQQQRdnTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNK 509
Cdd:cd18802 75 TQRKQKE--TLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPNSK 137
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
197-355 |
6.32e-08 |
|
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.
Pssm-ID: 350784 [Multi-domain] Cd Length: 202 Bit Score: 53.37 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 197 PVMLHGRELLASAPTGSGKTLAFSipILMqLKQPANKGFRALIISPTRELASQIHRELIKISEGTGFRI--HMIHKaava 274
Cdd:cd18026 28 PGLLEGRNLVYSLPTSGGKTLVAE--ILM-LKRLLERRKKALFVLPYVSIVQEKVDALSPLFEELGFRVegYAGNK---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 275 aKKFGPKSSKKFDILVTTP-------NRLIYLLKQDppgiDLASVewlVVDESDKLFEDGKTGFRDQLASIFLACTSHKV 347
Cdd:cd18026 101 -GRSPPKRRKSLSVAVCTIekanslvNSLIEEGRLD----ELGLV---VVDELHMLGDGHRGALLELLLTKLLYAAQKNI 172
|
....*...
gi 2203400809 348 RRAMFSAT 355
Cdd:cd18026 173 QIVGMSAT 180
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
169-373 |
6.36e-08 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 55.59 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 169 EYKINSRLLQNILDAGFQMPTPIQMQAIPV-MLHGRELLASAPTGSGKTLAFSIPILMQLKQpanKGFRALIISPTRELA 247
Cdd:PRK00254 5 ELRVDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLR---EGGKAVYLVPLKALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 248 SQIHRELiKISEGTGFRIHMIHkaavaakkfGPKSSK-----KFDILVTTPNRLIYLLKQDPPGIDlaSVEWLVVDESDK 322
Cdd:PRK00254 82 EEKYREF-KDWEKLGLRVAMTT---------GDYDSTdewlgKYDIIIATAEKFDSLLRHGSSWIK--DVKLVVADEIHL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400809 323 LfedgktGFRDQLASIFLACTsHKVRRAM---FSATF--AYDVEQWckLNLDNVIS 373
Cdd:PRK00254 150 I------GSYDRGATLEMILT-HMLGRAQilgLSATVgnAEELAEW--LNAELVVS 196
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
415-508 |
6.99e-08 |
|
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: 51.88 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 415 VLVFVQSIERAKELFHEL------IYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYD 488
Cdd:cd18796 41 TLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120
|
90 100
....*....|....*....|
gi 2203400809 489 FPTSSVEYIHRIGRTGRAGN 508
Cdd:cd18796 121 SPKSVARLLQRLGRSGHRPG 140
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
399-513 |
4.70e-07 |
|
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: 49.86 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 399 KLLAVRELVKKGfnpPVLVFVQSieR------AKEL----FHeliyeginvdviHAERTQQQRDnTVHS-FRAGKIWVLI 467
Cdd:cd18795 33 VLLKIETVSEGK---PVLVFCSS--RkecektAKDLagiaFH------------HAGLTREDRE-LVEElFREGLIKVLV 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203400809 468 CTALLArgidfKGVNL----VI----------NYDFPTSSvEYIHRIGRTGRAG--NKGKAI 513
Cdd:cd18795 95 ATSTLA-----AGVNLpartVIikgtqrydgkGYRELSPL-EYLQMIGRAGRPGfdTRGEAI 150
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
190-319 |
1.86e-06 |
|
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: 47.69 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 190 PIQMQAIPVML---HGRELLASAPTGSGKTLaFSIPILMQLKQpankgFRALIISPTRELASQIHRELIKISEGtgfriH 266
Cdd:cd17926 3 PYQEEALEAWLahkNNRRGILVLPTGSGKTL-TALALIAYLKE-----LRTLIVVPTDALLDQWKERFEDFLGD-----S 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2203400809 267 MIHkaavaakKFGPKSSKKFD---ILVTTPNRLIYLLKQDPPGIDLASVewLVVDE 319
Cdd:cd17926 72 SIG-------LIGGGKKKDFDdanVVVATYQSLSNLAEEEKDLFDQFGL--LIVDE 118
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
200-292 |
2.87e-06 |
|
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: 48.09 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 200 LHGRELLASAPTGSGKT---LAFSIPIlmqlkqpANKGFRALIISPTRELASQIHRELIKISEGTGFRIHMIHKAAVAAK 276
Cdd:cd17924 30 LRGKSFAIIAPTGVGKTtfgLATSLYL-------ASKGKRSYLIFPTKSLVKQAYERLSKYAEKAGVEVKILVYHSRLKK 102
|
90 100
....*....|....*....|.
gi 2203400809 277 KFGPKSSKK-----FDILVTT 292
Cdd:cd17924 103 KEKEELLEKiekgdFDILVTT 123
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
191-253 |
3.66e-06 |
|
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: 48.12 E-value: 3.66e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2203400809 191 IQMQAIPVMLHGRE-LLASAPTGSGKTLAFSIPILMQLKQPANKG---FRALIISPTRELASQIHRE 253
Cdd:cd18023 5 IQSEVFPDLLYSDKnFVVSAPTGSGKTVLFELAILRLLKERNPLPwgnRKVVYIAPIKALCSEKYDD 71
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
360-518 |
6.40e-06 |
|
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: 46.47 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 360 VEQWCKLNLDNVISVSIGARNSavetvEQELLFVGSeTGKLLAVRELVKKGFNP-PVLVFVQSIERAKElfhelIYEGIN 438
Cdd:cd18789 2 AEIRCPMTPEFYREYLGLGAHR-----KRRLLAAMN-PNKLRALEELLKRHEQGdKIIVFTDNVEALYR-----YAKRLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 439 VDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDF--KGVNLVINYDFpTSSVEYIHRIGRTGRAGNKGKAITFF 516
Cdd:cd18789 71 KPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLpeANVAIQISGHG-GSRRQEAQRLGRILRPKKGGGKNAFF 149
|
..
gi 2203400809 517 TE 518
Cdd:cd18789 150 YS 151
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
395-513 |
1.04e-05 |
|
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: 45.71 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 395 SETGKLLAvrELVKKGFNppVLVFVQS---IER-AKELFHELIYEGINVDVIHAER---TQQQRDNTVHSFRAGKIWVLI 467
Cdd:cd18797 22 REAARLFA--DLVRAGVK--TIVFCRSrklAELlLRYLKARLVEEGPLASKVASYRagyLAEDRREIEAELFNGELLGVV 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2203400809 468 CTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAI 513
Cdd:cd18797 98 ATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVI 143
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
188-264 |
1.08e-05 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 46.26 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 188 PTPIQMQAIPVMLHG------RELLASAPTGSGKTLAFSIPILMQLkqpaNKGFRALIISPTRELASQIHREL------I 255
Cdd:cd17918 16 LTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAY----KNGKQVAILVPTEILAHQHYEEArkflpfI 91
|
....*....
gi 2203400809 256 KISEGTGFR 264
Cdd:cd17918 92 NVELVTGGT 100
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
419-528 |
1.57e-05 |
|
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: 45.34 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 419 VQSIERAKELFHELIYEgINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIH 498
Cdd:cd18792 44 LKSIEALAEELKELVPE-ARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLH 122
|
90 100 110
....*....|....*....|....*....|.
gi 2203400809 499 RI-GRTGRAGNKGKAitFFTEDDKPLLRSVA 528
Cdd:cd18792 123 QLrGRVGRGKHQSYC--YLLYPDPKKLTETA 151
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
414-527 |
2.21e-05 |
|
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: 46.08 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 414 PVLVFV----QSIERA-KELFHEliYEGINVDVIHAeRTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLV--IN 486
Cdd:cd18804 94 EDLVFKgigtERVEEElKTLFPE--ARIARIDRDTT-RKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLN 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2203400809 487 YDFPTSSVEY---------IHRI-GRTGRAGNKGKAI--TFFTEDdkPLLRSV 527
Cdd:cd18804 171 ADSGLNSPDFraserafqlLTQVsGRAGRGDKPGKVIiqTYNPEH--PLIQAA 221
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
416-517 |
2.46e-05 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 43.70 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 416 LVFVQSIERAKELFHELIYEGINVDVIHAERTQQQR-DNTVHSFRAGKIW--VLICTALLARGIDFKGVNLVInYDFPT- 491
Cdd:cd18799 10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGELKppILVTVDLLTTGVDIPEVDNVV-FLRPTe 88
|
90 100
....*....|....*....|....*..
gi 2203400809 492 SSVEYIHRIGR-TGRAGNKgkaiTFFT 517
Cdd:cd18799 89 SRTLFLQMLGRgLRLHEGK----DFFT 111
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
190-319 |
2.99e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 47.26 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 190 PIQMQAIPV-MLHGRELLASAPTGSGKTLafsIPILMQLKQPANKGfRALIISPTRELASQIHRELIKISEgTGFRIhmi 268
Cdd:PRK02362 26 PPQAEAVEAgLLDGKNLLAAIPTASGKTL---IAELAMLKAIARGG-KALYIVPLRALASEKFEEFERFEE-LGVRV--- 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2203400809 269 hkaAVAAKKFGPKSS--KKFDILVTTPNRLIYLLKQDPPGIDLASVewLVVDE 319
Cdd:PRK02362 98 ---GISTGDYDSRDEwlGDNDIIVATSEKVDSLLRNGAPWLDDITC--VVVDE 145
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
175-319 |
3.27e-05 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 45.32 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 175 RLLQNILdaGFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIP-ILMQLKQPAnkgfRALIISPTREL-ASQIHR 252
Cdd:cd18018 2 KLLRRVF--GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPaLLLRRRGPG----LTLVVSPLIALmKDQVDA 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203400809 253 eLIKISEGTgfRIHMIHKAAVAAKKFGPKSSKKFDILVTTPNRL-----IYLLKQdPPGIDLasvewLVVDE 319
Cdd:cd18018 76 -LPRAIKAA--ALNSSLTREERRRILEKLRAGEVKILYVSPERLvnesfRELLRQ-TPPISL-----LVVDE 138
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
209-269 |
6.60e-05 |
|
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442728 [Multi-domain] Cd Length: 402 Bit Score: 45.75 E-value: 6.60e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400809 209 APTGSGKTLAFSIPILMQLKqpanKGFRALIISPTRELASQIHRELIKisegTGFRIHMIH 269
Cdd:COG3505 6 GPTGSGKTVGLVIPNLTQLA----RGESVVVTDPKGDLAELTAGFRRR----AGYDVYVFD 58
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
184-242 |
1.16e-04 |
|
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: 43.68 E-value: 1.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2203400809 184 GFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMqlkqpaNKGFrALIISP 242
Cdd:cd17920 9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALL------LDGV-TLVVSP 60
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
403-513 |
2.27e-04 |
|
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: 42.23 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 403 VRELVKKGFNppVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVN 482
Cdd:cd18790 20 IRKRVARGER--VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVS 97
|
90 100 110
....*....|....*....|....*....|....*.
gi 2203400809 483 LVINYD-----FPTSSVEYIHRIGRTGRAGNkGKAI 513
Cdd:cd18790 98 LVAILDadkegFLRSETSLIQTIGRAARNVN-GKVI 132
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
191-326 |
2.93e-04 |
|
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: 42.42 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 191 IQMQAIPVMLHGRE-LLASAPTGSGKTLAFSIPILMQLKQPANKG-------FRALIISPTRELASQIHREL-------- 254
Cdd:cd18020 5 IQSLVFPVAYKTNEnMLICAPTGAGKTNIAMLTILHEIRQHVNQGgvikkddFKIVYIAPMKALAAEMVEKFskrlaplg 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203400809 255 IKISEGTGfriHM-IHKAAVAAKKfgpksskkfdILVTTPNRLIYLLKQDPPGIDLAS-VEWLVVDESDKLFED 326
Cdd:cd18020 85 IKVKELTG---DMqLTKKEIAETQ----------IIVTTPEKWDVVTRKSSGDVALSQlVRLLIIDEVHLLHDD 145
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
188-319 |
3.16e-04 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 42.42 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 188 PTPIQMQAIPVMLHGRELLASAPTGSGKTLAfSIPILMQL--KQPANKGFRALIISPTRELASQIHRELIKISEGTGFRI 265
Cdd:cd17927 3 PRNYQLELAQPALKGKNTIICLPTGSGKTFV-AVLICEHHlkKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2203400809 266 HMIhKAAVAAKKFGPKSSKKFDILVTTPNRLIYLLKqDPPGIDLASVEWLVVDE 319
Cdd:cd17927 82 TGL-SGDTSENVSVEQIVESSDVIIVTPQILVNDLK-SGTIVSLSDFSLLVFDE 133
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
190-293 |
3.40e-04 |
|
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: 41.98 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 190 PIQMQAIPVMLHGRE-LLASAPTGSGKTLAFSIPILMQLKQpaNKGFRALIISPTRELAsqihRELI-----KISEGTGF 263
Cdd:cd18022 4 PIQTQVFHTLYHTDNnVLLGAPTGSGKTIAAELAMFRAFNK--YPGSKVVYIAPLKALV----RERVddwkkRFEEKLGK 77
|
90 100 110
....*....|....*....|....*....|
gi 2203400809 264 RIHMIHKAAVAakkfGPKSSKKFDILVTTP 293
Cdd:cd18022 78 KVVELTGDVTP----DMKALADADIIITTP 103
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
188-301 |
4.36e-04 |
|
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: 41.69 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 188 PTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQ--PANKGFRALIISPTRELASQIHRELIKISEGtGFRI 265
Cdd:cd18036 3 LRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKrrSAGEKGRVVVLVNKVPLVEQQLEKFFKYFRK-GYKV 81
|
90 100 110
....*....|....*....|....*....|....*.
gi 2203400809 266 HMIHkAAVAAKKFGPKSSKKFDILVTTPNRLIYLLK 301
Cdd:cd18036 82 TGLS-GDSSHKVSFGQIVKASDVIICTPQILINNLL 116
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
190-297 |
4.97e-04 |
|
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: 41.48 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 190 PIQMQAIPVMLHGRE-LLASAPTGSGKTLAFSIPILMQLKQPANKgfRALIISPTRELASQIHRELikisegtgfrihmi 268
Cdd:cd18021 6 PIQTQVFNSLYNTDDnVFVGAPTGSGKTVCAELALLRHWRQNPKG--RAVYIAPMQELVDARYKDW-------------- 69
|
90 100 110
....*....|....*....|....*....|..
gi 2203400809 269 hkaavaAKKFGPKSSKKFDIL---VTTPNRLI 297
Cdd:cd18021 70 ------RAKFGPLLGKKVVKLtgeTSTDLKLL 95
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
175-242 |
8.02e-04 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350773 [Multi-domain] Cd Length: 209 Bit Score: 41.20 E-value: 8.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 175 RLLQNIldagFQMPT--PIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMqlkqpaNKGFrALIISP 242
Cdd:cd18015 8 DTLKNV----FKLEKfrPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALC------SDGF-TLVVSP 66
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
184-525 |
8.26e-04 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 42.39 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 184 GFQMPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQlkqpanKGFrALIISPtrelasqihreLIKISEGtgf 263
Cdd:PRK11057 22 GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL------DGL-TLVVSP-----------LISLMKD--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 264 RIHMIHKAAVAAKKFGPKSSK-------------KFDILVTTPNRL-----IYLLKQDPPGIdlasvewLVVDESDKLFE 325
Cdd:PRK11057 81 QVDQLLANGVAAACLNSTQTReqqlevmagcrtgQIKLLYIAPERLmmdnfLEHLAHWNPAL-------LAVDEAHCISQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 326 DGKTgFRDQLASI-----------FLACTshkvrrAMFSATFAYDVEQwcKLNLDNVIsVSIGA------RNSAVET--- 385
Cdd:PRK11057 154 WGHD-FRPEYAALgqlrqrfptlpFMALT------ATADDTTRQDIVR--LLGLNDPL-IQISSfdrpniRYTLVEKfkp 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 386 VEQELLFVGSETGKllavrelvkKGfnppvLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWV 465
Cdd:PRK11057 224 LDQLMRYVQEQRGK---------SG-----IIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQI 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 466 LICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNKGKAITFFTEDDKPLLR 525
Cdd:PRK11057 290 VVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLR 349
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
201-343 |
8.59e-04 |
|
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438711 [Multi-domain] Cd Length: 174 Bit Score: 40.39 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 201 HGRELLaSAPTGSGKTLAfsIPILMqLKQPANKGFRALIISPTRELASQIHRELIK-----ISEGTGFRIHMIHkaavaa 275
Cdd:cd17990 17 GGQVVL-EAPPGAGKTTR--VPLAL-LAELWIAGGKIIVLEPRRVAARAAARRLATllgeaPGETVGYRVRGES------ 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400809 276 kkfgpKSSKKFDILVTTPNRLIYLLKQDPpgiDLASVEWLVVDE-------SDKLFE---DGKTGFRDQLASIFLACT 343
Cdd:cd17990 87 -----RVGRRTRVEVVTEGVLLRRLQRDP---ELSGVGAVILDEfhersldADLALAlllEVQQLLRDDLRLLAMSAT 156
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
201-319 |
8.78e-04 |
|
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins 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: 350677 [Multi-domain] Cd Length: 182 Bit Score: 40.63 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 201 HGRELLASAPtGSGKTLAfSIPILMQLKQPANKGFRALIISPtrelASQIH---RELIKISEGtgFRIHMIHKA-AVAAK 276
Cdd:cd17919 19 GPGGILADEM-GLGKTLQ-AIAFLAYLLKEGKERGPVLVVCP----LSVLEnweREFEKWTPD--LRVVVYHGSqRERAQ 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2203400809 277 KFGPKSSKKFDILVTTPNRLIYLLKQdppgidLASVEW--LVVDE 319
Cdd:cd17919 91 IRAKEKLDKFDVVLTTYETLRRDKAS------LRKFRWdlVVVDE 129
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
190-257 |
9.92e-04 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 42.23 E-value: 9.92e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203400809 190 PIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQpankGFRALIISPTRELASQIHRELIKI 257
Cdd:COG4581 28 PFQEEAILALEAGRSVLVAAPTGSGKTLVAEFAIFLALAR----GRRSFYTAPIKALSNQKFFDLVER 91
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
209-246 |
1.55e-03 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 39.13 E-value: 1.55e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2203400809 209 APTGSGKTLAFSIPILMQlkqpANKGFRALIISPTREL 246
Cdd:cd01127 6 GTTGSGKTTSIVIPLLDQ----AARGGSVIITDPKGEL 39
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
443-504 |
1.80e-03 |
|
putative ATP-dependent helicase Lhr; Provisional
Pssm-ID: 137505 [Multi-domain] Cd Length: 1490 Bit Score: 41.45 E-value: 1.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203400809 443 HAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTG 504
Cdd:PRK09751 308 HGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| DEAHc_XPD-like |
cd17915 |
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ... |
209-323 |
2.05e-03 |
|
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D (XPD)-like family members 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: 350673 [Multi-domain] Cd Length: 138 Bit Score: 38.95 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 209 APTGSGKTLaFSIPILMQLkQPANKGFRALIISPTRELASQIHRELIKISEGTGFRihmihkaavaakkFGPKSSKKFDI 288
Cdd:cd17915 8 SPTGSGKTL-SLLCSALSY-QREFHKTKVLYCSRTHSQIEQIIRELRKLLEKRKIR-------------ALALSSRDADI 72
|
90 100 110
....*....|....*....|....*....|....*
gi 2203400809 289 LVTTPNRLIYLLKQDPPGIDLaSVEWLVVDESDKL 323
Cdd:cd17915 73 VVLPYPYLLDARIREFIGIDL-REQVVIIDEAHNL 106
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
206-319 |
2.72e-03 |
|
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: 39.56 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 206 LASAPTGSGKTLafsIPILM------QLKQPANKGFRALIISPTRELASQIHRElikISEGTGFRIHMIHKAAVAAKKFG 279
Cdd:cd18034 20 IVVLPTGSGKTL---IAVMLikemgeLNRKEKNPKKRAVFLVPTVPLVAQQAEA---IRSHTDLKVGEYSGEMGVDKWTK 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2203400809 280 PKSS---KKFDILVTTPNRLIYLLKQdppG-IDLASVEWLVVDE 319
Cdd:cd18034 94 ERWKeelEKYDVLVMTAQILLDALRH---GfLSLSDINLLIFDE 134
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
188-320 |
3.42e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 38.42 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203400809 188 PTPIQMQAI----PVMLHGRE-LLASAPTGSGKTL-AFSIpilMQLKQPANKGFRALIISPTRELASQIHRELIKISEGT 261
Cdd:pfam04851 4 LRPYQIEAIenllESIKNGQKrGLIVMATGSGKTLtAAKL---IARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFLPNY 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203400809 262 GFRIhmihkaAVAAKKFGPKSSKKFDILVTTPNRL--IYLLKQDPPGIDLASVewLVVDES 320
Cdd:pfam04851 81 VEIG------EIISGDKKDESVDDNKIVVTTIQSLykALELASLELLPDFFDV--IIIDEA 133
|
|
| |
