|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
163-534 |
6.83e-120 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 361.39 E-value: 6.83e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 163 TFQQLdqeyKISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQPTNKGFRALVIS 242
Cdd:COG0513 3 SFADL----GLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRAPQALILA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 243 PTRELASQIHRELIKISEGTGFRIHMIH-----KAAIAAKKFGPksskkfDILVTTPNRLIYLLKQEppGIDLTSVEWLV 317
Cdd:COG0513 79 PTRELALQVAEELRKLAKYLGLRVATVYggvsiGRQIRALKRGV------DIVVATPGRLLDLIERG--ALDLSGVETLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 318 VDESDKLFEDGktgFRDQLASIfLACTSPKVRRAMFSATFAYDVEQWCKLNLDNIVSVSIGARNSAVETVEQELLFVGSE 397
Cdd:COG0513 151 LDEADRMLDMG---FIEDIERI-LKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 398 TgKLLAMRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGI 477
Cdd:COG0513 227 D-KLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGI 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 16758984 478 DFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNRGKAVTFFTEDDKPLLRSVANVIQQ 534
Cdd:COG0513 306 DIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQ 362
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
177-378 |
1.94e-112 |
|
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: 334.17 E-value: 1.94e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 177 LLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQP-TNKGFRALVISPTRELASQIHREL 255
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPrKKKGLRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 256 IKISEGTGFRIHMIHKAAIAAKKFGPKSSKKFDILVTTPNRLIYLLKQEPpgIDLTSVEWLVVDESDKLFEdgkTGFRDQ 335
Cdd:cd17957 81 LKLSKGTGLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGP--IDLSSVEYLVLDEADKLFE---PGFREQ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16758984 336 LASIFLACTSPKVRRAMFSATFAYDVEQWCKLNLDNIVSVSIG 378
Cdd:cd17957 156 TDEILAACTNPNLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
136-540 |
1.01e-79 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 260.49 E-value: 1.01e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 136 LRKEKINFFRNKHKIHVQGTDLPDPIATFQQLdqeyKISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSG 215
Cdd:PLN00206 95 LSSSQAELLRRKLEIHVKGEAVPPPILSFSSC----GLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 216 KTLAFSIPILMQLKQ------PTNKGFRALVISPTRELASQIHRELIKISEGTGFRIHMIHKAAIAAKKFgPKSSKKFDI 289
Cdd:PLN00206 171 KTASFLVPIISRCCTirsghpSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQL-YRIQQGVEL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 290 LVTTPNRLIYLLKQEppGIDLTSVEWLVVDESDKLFEdgkTGFRDQLASIFLACTSPKVrrAMFSATFAYDVEQWCKLNL 369
Cdd:PLN00206 250 IVGTPGRLIDLLSKH--DIELDNVSVLVLDEVDCMLE---RGFRDQVMQIFQALSQPQV--LLFSATVSPEVEKFASSLA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 370 DNIVSVSIGARNSAVETVEQELLFVGSETGKLLAMRELVKKG-FNPPVLVFVQSIERAkELFHELI--YEGINVDVIHAE 446
Cdd:PLN00206 323 KDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSKQhFKPPAVVFVSSRLGA-DLLANAItvVTGLKALSIHGE 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 447 RTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNRGKAVTFFTEDDKPLLR 526
Cdd:PLN00206 402 KSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFP 481
|
410
....*....|....
gi 16758984 527 SVANVIQQAGCPVP 540
Cdd:PLN00206 482 ELVALLKSSGAAIP 495
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
126-540 |
1.72e-69 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 234.28 E-value: 1.72e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 126 KKLTSEKLEHLRKEkinffrnkHKIH-VQGTDLPDPIATFqqldqEYKISPR-LLQNILDAGFQVPTPIQMQAIPVMLHG 203
Cdd:PTZ00110 101 SALSSKEVDEIRKE--------KEITiIAGENVPKPVVSF-----EYTSFPDyILKSLKNAGFTEPTPIQVQGWPIALSG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 204 RELLASAPTGSGKTLAFSIPILMQLK-QPTNK---GFRALVISPTRELASQIHRELIKIseGTGFRIHmiHKAAiaakkF 279
Cdd:PTZ00110 168 RDMIGIAETGSGKTLAFLLPAIVHINaQPLLRygdGPIVLVLAPTRELAEQIREQCNKF--GASSKIR--NTVA-----Y 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 280 G--PKSSKKF------DILVTTPNRLIYLLKQEPpgIDLTSVEWLVVDESDKLFEdgkTGFRDQLASIfLACTSPKVRRA 351
Cdd:PTZ00110 239 GgvPKRGQIYalrrgvEILIACPGRLIDFLESNV--TNLRRVTYLVLDEADRMLD---MGFEPQIRKI-VSQIRPDRQTL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 352 MFSATFAYDVEQWCK-LNLDNIVSVSIGARN-SAVETVEQELlFVGSETGKLLAMRELVKKGF--NPPVLVFVQSIERAK 427
Cdd:PTZ00110 313 MWSATWPKEVQSLARdLCKEEPVHVNVGSLDlTACHNIKQEV-FVVEEHEKRGKLKMLLQRIMrdGDKILIFVETKKGAD 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 428 ELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRA 507
Cdd:PTZ00110 392 FLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRA 471
|
410 420 430
....*....|....*....|....*....|...
gi 16758984 508 GNRGKAVTFFTEDDKPLLRSVANVIQQAGCPVP 540
Cdd:PTZ00110 472 GAKGASYTFLTPDKYRLARDLVKVLREAKQPVP 504
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
173-534 |
1.10e-65 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 221.61 E-value: 1.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 173 ISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL--KQPTNKG---FRALVISPTREL 247
Cdd:PRK10590 8 LSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLitRQPHAKGrrpVRALILTPTREL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 248 ASQIHRELIKISEGTGFRIHMIhkaaiaakkFG-----PKSSK---KFDILVTTPNRLIYLLKQEppGIDLTSVEWLVVD 319
Cdd:PRK10590 88 AAQIGENVRDYSKYLNIRSLVV---------FGgvsinPQMMKlrgGVDVLVATPGRLLDLEHQN--AVKLDQVEILVLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 320 ESDKLFEdgkTGFRDQLASIfLACTSPKVRRAMFSATFAYDVEQWCKLNLDNIVSVSIGARNSAVETVEQELLFVGSETG 399
Cdd:PRK10590 157 EADRMLD---MGFIHDIRRV-LAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 400 KLLaMRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDF 479
Cdd:PRK10590 233 REL-LSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDI 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 16758984 480 KGVNLVINYDFPTSSVEYIHRIGRTGRAGNRGKAVTFFTEDDKPLLRSVANVIQQ 534
Cdd:PRK10590 312 EELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKK 366
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
169-540 |
3.61e-64 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 218.24 E-value: 3.61e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 169 QEYKISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQ--PTNKGF----RALVIS 242
Cdd:PRK01297 90 HDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQtpPPKERYmgepRALIIA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 243 PTRELASQIHRELIKISEGTGFRIHMIHKAAIAAKKFGPKSSKKFDILVTTPNRLIYLLKQEPPGIDLtsVEWLVVDESD 322
Cdd:PRK01297 170 PTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEARFCDILVATPGRLLDFNQRGEVHLDM--VEVMVLDEAD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 323 KLFEdgkTGFRDQLASIfLACTSPKVRRA--MFSATFAYDVEQWCKLNLDNIVSVSIGARNSAVETVEQELLFV-GSETG 399
Cdd:PRK01297 248 RMLD---MGFIPQVRQI-IRQTPRKEERQtlLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVaGSDKY 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 400 KLLamRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDF 479
Cdd:PRK01297 324 KLL--YNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHI 401
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758984 480 KGVNLVINYDFPTSSVEYIHRIGRTGRAGNRGKAVTFFTEDDKPLLRSVANVI-QQAGCPVP 540
Cdd:PRK01297 402 DGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLgRKISCEMP 463
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
177-376 |
2.20e-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: 2.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 177 LLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL---KQPTNKGFRALVISPTRELASQIHR 253
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLlpePKKKGRGPQALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 254 ELIKISEGTGFRIHMI-----HKAAIAAKKfgpkssKKFDILVTTPNRLIYLLKQEPpgIDLTSVEWLVVDESDKLFEDg 328
Cdd:cd00268 81 VARKLGKGTGLKVAAIyggapIKKQIEALK------KGPDIVVGTPGRLLDLIERGK--LDLSNVKYLVLDEADRMLDM- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16758984 329 ktGFRDQLASIFLACtSPKVRRAMFSATFAYDVEQWCKLNLDNIVSVS 376
Cdd:cd00268 152 --GFEEDVEKILSAL-PKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
163-591 |
4.08e-61 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 209.03 E-value: 4.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 163 TFQQLDqeykISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL-----KQPtnkGF- 236
Cdd:PRK11192 2 TFSELE----LDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLldfprRKS---GPp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 237 RALVISPTRELASQIHRELIKISEGTGFRIHMIhKAAIAAKKFGPKSSKKFDILVTTPNRLIYLLKQEppGIDLTSVEWL 316
Cdd:PRK11192 75 RILILTPTRELAMQVADQARELAKHTHLDIATI-TGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEE--NFDCRAVETL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 317 VVDESDKLFEdgkTGFRDQLASIFLACTSPKvRRAMFSAT--------FAYDVeqwcklnLDNIVSVSIGARNSAVETVE 388
Cdd:PRK11192 152 ILDEADRMLD---MGFAQDIETIAAETRWRK-QTLLFSATlegdavqdFAERL-------LNDPVEVEAEPSRRERKKIH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 389 QELLFVGSETGK--LLA---MRELVKKGFnppvlVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGK 463
Cdd:PRK11192 221 QWYYRADDLEHKtaLLChllKQPEVTRSI-----VFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 464 IWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNRGKAVTFFTEDDKPLLRSVANVIQQagcPV-PEY 542
Cdd:PRK11192 296 VNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEE---PLkARV 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 16758984 543 IKGFqkllskqkKKMIKKPLERESISTTPKYFLEQAKQKKVAGQNSKKK 591
Cdd:PRK11192 373 IDEL--------RPKTKAPSEKKTGKPSKKVLAKRAEKKEKEKEKPKVK 413
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
174-521 |
1.86e-57 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 199.64 E-value: 1.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 174 SPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLkQPTNKGFRALVISPTRELASQIHR 253
Cdd:PRK11776 12 PPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL-DVKRFRVQALVLCPTRELADQVAK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 254 EL---------IKI---SEGTGFRIHmihkaaIAAKKFGPKsskkfdILVTTPNRLIYLLKQEppGIDLTSVEWLVVDES 321
Cdd:PRK11776 91 EIrrlarfipnIKVltlCGGVPMGPQ------IDSLEHGAH------IIVGTPGRILDHLRKG--TLDLDALNTLVLDEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 322 DKLFEdgkTGFRDQLASIFLACtsPKVRRAM-FSATFAYDVEQWCKLNLDNIVSVSIGARNSAvETVEQELLFVgSETGK 400
Cdd:PRK11776 157 DRMLD---MGFQDAIDAIIRQA--PARRQTLlFSATYPEGIAAISQRFQRDPVEVKVESTHDL-PAIEQRFYEV-SPDER 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 401 LLAMRELVKKgFNP-PVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDF 479
Cdd:PRK11776 230 LPALQRLLLH-HQPeSCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDI 308
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 16758984 480 KGVNLVINYDFPTSSVEYIHRIGRTGRAGNRGKAVTFFTEDD 521
Cdd:PRK11776 309 KALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEE 350
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
387-517 |
3.25e-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: 183.09 E-value: 3.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 387 VEQELLFVGSETGKLLAMRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWV 466
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 16758984 467 LICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNRGKAVTFF 517
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
155-519 |
3.14e-47 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 174.37 E-value: 3.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 155 TDLPDPIATFQQLDqeykISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL------ 228
Cdd:PRK04537 2 SDKPLTDLTFSSFD----LHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLlsrpal 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 229 --KQPTNKgfRALVISPTRELASQIHRELIKISEGTGFRIHMIHkAAIAAKKFGPKSSKKFDILVTTPNRLIYLLKQEPP 306
Cdd:PRK04537 78 adRKPEDP--RALILAPTRELAIQIHKDAVKFGADLGLRFALVY-GGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 307 gIDLTSVEWLVVDESDKLFEdgkTGFRDQLASIFLACTSPKVRRAM-FSATFAYDVEQWCKLNLDNIVSVSIGARNSAVE 385
Cdd:PRK04537 155 -VSLHACEICVLDEADRMFD---LGFIKDIRFLLRRMPERGTRQTLlFSATLSHRVLELAYEHMNEPEKLVVETETITAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 386 TVEQELLFVGSETgKLLAMRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIW 465
Cdd:PRK04537 231 RVRQRIYFPADEE-KQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLE 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 16758984 466 VLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNRGKAVTFFTE 519
Cdd:PRK04537 310 ILVATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACE 363
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
177-376 |
2.08e-46 |
|
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: 162.04 E-value: 2.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 177 LLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL--KQPTNKGFRALVISPTRELASQIHRE 254
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLlyRPKKKAATRVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 255 LIKISEGTGFRIHMI-----HKAAIAAKKFGPksskkfDILVTTPNRLIYLLKQEpPGIDLTSVEWLVVDESDKLFEDgk 329
Cdd:cd17947 81 LQQLAQFTDITFALAvgglsLKAQEAALRARP------DIVIATPGRLIDHLRNS-PSFDLDSIEILVLDEADRMLEE-- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16758984 330 tGFRDQLASIFLACtsPKVRRAM-FSATFAYDVEQWCKLNLDNIVSVS 376
Cdd:cd17947 152 -GFADELKEILRLC--PRTRQTMlFSATMTDEVKDLAKLSLNKPVRVF 196
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
173-520 |
4.41e-46 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 167.84 E-value: 4.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 173 ISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAF-----------SIPILMQLKQPtnkgfRALVI 241
Cdd:PRK04837 15 LHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFltatfhyllshPAPEDRKVNQP-----RALIM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 242 SPTRELASQIHRELIKISEGTGFrihmihKAAIAakkFGPKSSKK--------FDILVTTPNRLIYLLKQEPpgIDLTSV 313
Cdd:PRK04837 90 APTRELAVQIHADAEPLAQATGL------KLGLA---YGGDGYDKqlkvlesgVDILIGTTGRLIDYAKQNH--INLGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 314 EWLVVDESDKLFEdgkTGFRDQLASIFLACTSPKVRRAM-FSATFAYDVEQWCKLNLDNIVSVSIGARNSAVETVEQELl 392
Cdd:PRK04837 159 QVVVLDEADRMFD---LGFIKDIRWLFRRMPPANQRLNMlFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEEL- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 393 FVGSETGKLLAMRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTAL 472
Cdd:PRK04837 235 FYPSNEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDV 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 16758984 473 LARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNRGKAVTFFTED 520
Cdd:PRK04837 315 AARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEE 362
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
173-528 |
1.27e-45 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 170.80 E-value: 1.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 173 ISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKqPTNKGFRALVISPTRELASQIH 252
Cdd:PRK11634 13 LKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLD-PELKAPQILVLAPTRELAVQVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 253 RELikisegTGFRIHMIHKAAIA------------AKKFGPKsskkfdILVTTPNRLIYLLKQEPpgIDLTSVEWLVVDE 320
Cdd:PRK11634 92 EAM------TDFSKHMRGVNVVAlyggqrydvqlrALRQGPQ------IVVGTPGRLLDHLKRGT--LDLSKLSGLVLDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 321 SDKLFedgKTGFRDQLASIfLACTSPKVRRAMFSATFAYDVEQWCKLNLDNIVSVSIGARNSAVETVEQELLFVGSETGK 400
Cdd:PRK11634 158 ADEML---RMGFIEDVETI-MAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 401 LLAMRELVKKGFNPPVlVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFK 480
Cdd:PRK11634 234 EALVRFLEAEDFDAAI-IFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 16758984 481 GVNLVINYDFPTSSVEYIHRIGRTGRAGNRGKAVTFFTEDDKPLLRSV 528
Cdd:PRK11634 313 RISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNI 360
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
163-356 |
1.54e-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: 159.78 E-value: 1.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 163 TFQQLDqeykISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQP-TNKGFRALVI 241
Cdd:cd17959 2 GFQSMG----LSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHsPTVGARALIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 242 SPTRELASQIHRELIKISEGTGFRIHMIHKAAIAAKKFGPKSSKKfDILVTTPNRLIYLLKQEppGIDLTSVEWLVVDES 321
Cdd:cd17959 78 SPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNP-DIIIATPGRLLHLLVEM--NLKLSSVEYVVFDEA 154
|
170 180 190
....*....|....*....|....*....|....*
gi 16758984 322 DKLFEdgkTGFRDQLASIfLACTSPKVRRAMFSAT 356
Cdd:cd17959 155 DRLFE---MGFAEQLHEI-LSRLPENRQTLLFSAT 185
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
172-530 |
3.56e-45 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 165.00 E-value: 3.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 172 KISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILmQLKQPTNKGFRALVISPTRELASQI 251
Cdd:PTZ00424 34 KLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAAL-QLIDYDLNACQALILAPTRELAQQI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 252 HRELIKISEGTGFRIHMIHKAAIAAKKFGpKSSKKFDILVTTPNRLIYLLKQEPPGIDltSVEWLVVDESDKLFEdgkTG 331
Cdd:PTZ00424 113 QKVVLALGDYLKVRCHACVGGTVVRDDIN-KLKAGVHMVVGTPGRVYDMIDKRHLRVD--DLKLFILDEADEMLS---RG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 332 FRDQLASIFLAcTSPKVRRAMFSATFAYDVEQWCKLNLDNIVSVSIGARNSAVETVEQELLFVGSETGKLLAMRELVKKG 411
Cdd:PTZ00424 187 FKGQIYDVFKK-LPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQFYVAVEKEEWKFDTLCDLYETL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 412 FNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFP 491
Cdd:PTZ00424 266 TITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLP 345
|
330 340 350
....*....|....*....|....*....|....*....
gi 16758984 492 TSSVEYIHRIGRTGRAGNRGKAVTFFTEDDKPLLRSVAN 530
Cdd:PTZ00424 346 ASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIER 384
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
190-363 |
4.19e-44 |
|
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: 154.71 E-value: 4.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 190 TPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKqPTNKGFRALVISPTRELASQIHRELIKISEGTGFRIHMI 269
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALD-KLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 270 HKAAIAAKKFgpKSSKKFDILVTTPNRLIYLLKQEPpgiDLTSVEWLVVDESDKLFEDgktGFRDQLASIfLACTSPKVR 349
Cdd:pfam00270 80 LGGDSRKEQL--EKLKGPDILVGTPGRLLDLLQERK---LLKNLKLLVLDEAHRLLDM---GFGPDLEEI-LRRLPKKRQ 150
|
170
....*....|....
gi 16758984 350 RAMFSATFAYDVEQ 363
Cdd:pfam00270 151 ILLLSATLPRNLED 164
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
163-378 |
1.67e-43 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes Drosophila melanogaster Vasa, which is essential for development. DEAD box protein 3 (DDX3) has been reported to display a high level of RNA-independent ATPase activity stimulated by both RNA and DNA. DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DDX3 and DDX4 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350725 [Multi-domain] Cd Length: 221 Bit Score: 154.95 E-value: 1.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 163 TFQQLDqeykISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL---KQPTNKGFR-- 237
Cdd:cd17967 1 SFEEAG----LRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLledGPPSVGRGRrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 238 ----ALVISPTRELASQIHRELIKISEGTGFRI-------HMIHKAAiaakkfgpKSSKKFDILVTTPNRLIYLLKQEPp 306
Cdd:cd17967 77 aypsALILAPTRELAIQIYEEARKFSYRSGVRSvvvyggaDVVHQQL--------QLLRGCDILVATPGRLVDFIERGR- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758984 307 gIDLTSVEWLVVDESDKLFEdgkTGFRDQLASIFLACTSPKV--RR-AMFSATFAYDVEQWCKLNLDNIVSVSIG 378
Cdd:cd17967 148 -ISLSSIKFLVLDEADRMLD---MGFEPQIRKIVEHPDMPPKgeRQtLMFSATFPREIQRLAADFLKNYIFLTVG 218
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
181-390 |
3.26e-43 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 153.42 E-value: 3.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 181 ILDAGFQVPTPIQMQAIPVMLHG-RELLASAPTGSGKTLAFSIPILMQLKQptNKGFRALVISPTRELASQIHRELIKIS 259
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKR--GKGGRVLVLVPTRELAEQWAEELKKLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 260 EGTGFRIHMIHKAAIAAKKFGPKSSKKFDILVTTPNRLIYLLKQEPpgIDLTSVEWLVVDESDKLFEDgktGFRDQLASI 339
Cdd:smart00487 79 PSLGLKVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENDK--LSLSNVDLVILDEAHRLLDG---GFGDQLEKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16758984 340 fLACTSPKVRRAMFSATFAYDVEQWCKLNLDNIVSVSIGarNSAVETVEQE 390
Cdd:smart00487 154 -LKLLPKNVQLLLLSATPPEEIENLLELFLNDPVFIDVG--FTPLEPIEQF 201
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
152-375 |
2.42e-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: 143.67 E-value: 2.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 152 VQGTDLPDPIATFQQLDqeykISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLK-Q 230
Cdd:cd17953 2 VRGKDCPKPIQKWSQCG----LSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKdQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 231 PTNK---GFRALVISPTRELASQIHRELIKISEGTGFRIHMIHKAA-----IAAKKFGPksskkfDILVTTPNRLIYLLK 302
Cdd:cd17953 78 RPVKpgeGPIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSgiseqIAELKRGA------EIVVCTPGRMIDILT 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16758984 303 QEPPGI-DLTSVEWLVVDESDKLFEdgkTGFRDQLASIFLAcTSPKVRRAMFSATFAYDVEQWCKLNLDNIVSV 375
Cdd:cd17953 152 ANNGRVtNLRRVTYVVLDEADRMFD---MGFEPQIMKIVNN-IRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
183-377 |
5.32e-38 |
|
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: 138.96 E-value: 5.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 183 DAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL---KQPTNKGFRALVISPTRELASQIHRELIKIS 259
Cdd:cd17941 7 EAGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLyreRWTPEDGLGALIISPTRELAMQIFEVLRKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 260 EGTGFRIHMIhkaaIAAKKFGPKSSK--KFDILVTTPNRLIYLLkQEPPGIDLTSVEWLVVDESDKLFEdgkTGFRDQLA 337
Cdd:cd17941 87 KYHSFSAGLI----IGGKDVKEEKERinRMNILVCTPGRLLQHM-DETPGFDTSNLQMLVLDEADRILD---MGFKETLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16758984 338 SIFlaCTSPKVRRAM-FSATFAYDVEQWCKLNLDNIVSVSI 377
Cdd:cd17941 159 AIV--ENLPKSRQTLlFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
177-376 |
1.29e-37 |
|
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: 138.09 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 177 LLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL----KQPTNKGFRALVISPTRELASQIH 252
Cdd:cd17960 1 ILDVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkANLKKGQVGALIISPTRELATQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 253 RELIKISEGTGFRIH---MIHKAAIAA--KKFgpkSSKKFDILVTTPNRLIYLLKQEPPGIDLTSVEWLVVDESDKLFEd 327
Cdd:cd17960 81 EVLQSFLEHHLPKLKcqlLIGGTNVEEdvKKF---KRNGPNILVGTPGRLEELLSRKADKVKVKSLEVLVLDEADRLLD- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16758984 328 gkTGFRDQLASIfLACTsPKVRR-AMFSATFAYDVEQWCKLNLDNIVSVS 376
Cdd:cd17960 157 --LGFEADLNRI-LSKL-PKQRRtGLFSATQTDAVEELIKAGLRNPVRVV 202
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
141-363 |
4.65e-37 |
|
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: 138.56 E-value: 4.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 141 INFFRNKH-KIHVQGTDLPDPIATFQqldqEYKISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLA 219
Cdd:cd18052 21 INFDKYDEiPVEVTGRNPPPAILTFE----EANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 220 FSIPILMQLKQ-----PTNKGFR---ALVISPTRELASQIHRELIKISEGTGFR-------IHMIHKAAiaakkfgpKSS 284
Cdd:cd18052 97 FLLPVLTGMMKegltaSSFSEVQepqALIVAPTRELANQIFLEARKFSYGTCIRpvvvyggVSVGHQIR--------QIE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 285 KKFDILVTTPNRLIYLLKQEPpgIDLTSVEWLVVDESDKLFEdgkTGFRDQLASIFLACTSP-KVRRA--MFSATFAYDV 361
Cdd:cd18052 169 KGCHILVATPGRLLDFIGRGK--ISLSKLKYLILDEADRMLD---MGFGPEIRKLVSEPGMPsKEDRQtlMFSATFPEEI 243
|
..
gi 16758984 362 EQ 363
Cdd:cd18052 244 QR 245
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
177-371 |
5.80e-36 |
|
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: 134.68 E-value: 5.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 177 LLQNILDAGFQVPTPIQMQAIPVML---------HGRELLASAPTGSGKTLAFSIPILMQLKQPTNKGFRALVISPTREL 247
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLpsskstppyRPGDLCVSAPTGSGKTLAYVLPIVQALSKRVVPRLRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 248 ASQIHRELIKISEGTGFRIHMI-------HKAAIAAKKFGPKSSKKFDILVTTPNRLIYLLKqEPPGIDLTSVEWLVVDE 320
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVVSLsgqksfkKEQKLLLVDTSGRYLSRVDILVATPGRLVDHLN-STPGFTLKHLRFLVIDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758984 321 SDKL----------------FEDGKTGFRDQLASIFLACTSPKVRRAMFSATFAYDVEQWCKLNLDN 371
Cdd:cd17956 160 ADRLlnqsfqdwletvmkalGRPTAPDLGSFGDANLLERSVRPLQKLLFSATLTRDPEKLSSLKLHR 226
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
177-376 |
1.09e-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: 130.52 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 177 LLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL-KQP------TNKGFRALVISPTRELAS 249
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYIsRLPpldeetKDDGPYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 250 QIHRELIKISEGTGFR-IHMIHKAAIAAKKFgpKSSKKFDILVTTPNRLIYLLkqEPPGIDLTSVEWLVVDESDKLFEdg 328
Cdd:cd17945 81 QIEEETQKFAKPLGIRvVSIVGGHSIEEQAF--SLRNGCEILIATPGRLLDCL--ERRLLVLNQCTYVVLDEADRMID-- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758984 329 kTGFRDQLASIF-----------------LACTSPKVRRA--MFSATFAYDVEQWCKLNLDNIVSVS 376
Cdd:cd17945 155 -MGFEPQVTKILdampvsnkkpdteeaekLAASGKHRYRQtmMFTATMPPAVEKIAKGYLRRPVVVT 220
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
177-376 |
1.48e-34 |
|
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: 129.46 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 177 LLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL-KQPT---NKGFRALVISPTRELASQIH 252
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHImDQRElekGEGPIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 253 RELIKISEGTGFRIHMIHKAaiAAKKFGPKSSKK-FDILVTTPNRLIYLLKQEppGIDLTSVEWLVVDESDKLFEdgkTG 331
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGG--GSKWEQAKALQEgAEIVVATPGRLIDMVKKK--ATNLQRVTYLVLDEADRMFD---MG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16758984 332 FRDQLASIfLACTSPKVRRAMFSATFAYDVEQWCKLNLDNIVSVS 376
Cdd:cd17952 154 FEYQVRSI-VGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRVV 197
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
399-508 |
2.04e-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: 126.17 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 399 GKLLAMRELVKKGFNPPVLVFVQSIERAK-ELFHELiyEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGI 477
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEaELLLEK--EGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 16758984 478 DFKGVNLVINYDFPTSSVEYIHRIGRTGRAG 508
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
173-369 |
2.35e-34 |
|
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: 129.63 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 173 ISPRLLQNILDAGFQVPTPIQMQAIPVML-HGRELLASAPTGSGKTLAFSIP----ILMQLKQPTNKGFRALVISPTREL 247
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPaiqsLLNTKPAGRRSGVSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 248 ASQIHRELIKISEG-TGFRIHM------IHKAAIAAKKFGPksskkfDILVTTPNRLIYLLKQEPPGIDLTSVEWLVVDE 320
Cdd:cd17964 81 ALQIAAEAKKLLQGlRKLRVQSavggtsRRAELNRLRRGRP------DILVATPGRLIDHLENPGVAKAFTDLDYLVLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16758984 321 SDKLFEDgktGFRDQLASIfLACTSPKVRR----AMFSATFAYDVEQWCKLNL 369
Cdd:cd17964 155 ADRLLDM---GFRPDLEQI-LRHLPEKNADprqtLLFSATVPDEVQQIARLTL 203
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
175-375 |
5.50e-34 |
|
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: 128.09 E-value: 5.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 175 PRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPIL---MQLKQ--PTNKGFRALVISPTRELAS 249
Cdd:cd17961 3 PRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIqkiLKAKAesGEEQGTRALILVPTRELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 250 QIHRELIKISEGTGFRIHMIH---KAAIAAKKfgPKSSKKFDILVTTPNRLIYLLKQEPPgIDLTSVEWLVVDESDKLFe 326
Cdd:cd17961 83 QVSKVLEQLTAYCRKDVRVVNlsaSSSDSVQR--ALLAEKPDIVVSTPARLLSHLESGSL-LLLSTLKYLVIDEADLVL- 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16758984 327 dgKTGFRDQLASifLACTSPKVRRA-MFSATFAYDVEQWCKLNLDNIVSV 375
Cdd:cd17961 159 --SYGYEEDLKS--LLSYLPKNYQTfLMSATLSEDVEALKKLVLHNPAIL 204
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
154-378 |
7.63e-34 |
|
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: 129.39 E-value: 7.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 154 GTDLPDPIATFQQLDqeykISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQ------ 227
Cdd:cd18051 13 GENCPPHIETFSDLD----LGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQiyeqgp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 228 ---LKQPTNKGFR------ALVISPTRELASQIHRELIKISEGTGFRIHMIHKAAIAAKKFgpkssKKFD----ILVTTP 294
Cdd:cd18051 89 gesLPSESGYYGRrkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQM-----RDLErgchLLVATP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 295 NRLIYLLKQEPPGIDltSVEWLVVDESDKLFEdgkTGFRDQLASIFLACTSPK--VRRA-MFSATFAYDVEQWCKLNLDN 371
Cdd:cd18051 164 GRLVDMLERGKIGLD--YCKYLVLDEADRMLD---MGFEPQIRRIVEQDTMPPtgERQTlMFSATFPKEIQMLARDFLDN 238
|
....*..
gi 16758984 372 IVSVSIG 378
Cdd:cd18051 239 YIFLAVG 245
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
177-368 |
1.18e-33 |
|
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: 128.13 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 177 LLQNILDAGFQVPTPIQMQAIPV-MLHGRELLASAPTGSGKTLAFSIPIL---MQLKQ-----PTNKGFRALVISPTREL 247
Cdd:cd17946 1 ILRALADLGFSEPTPIQALALPAaIRDGKDVIGAAETGSGKTLAFGIPILerlLSQKSsngvgGKQKPLRALILTPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 248 ASQIHRELIKISEGTGFRIhMIHKAAIAAKKFGPKSSKKFDILVTTPNRLIYLLKQEPPGID-LTSVEWLVVDESDKLFE 326
Cdd:cd17946 81 AVQVKDHLKAIAKYTNIKI-ASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLAnLKSLRFLVLDEADRMLE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16758984 327 DGKtgFRDqLASIF------LACTSPKVRRAMFSATFAYDVEQWCKLN 368
Cdd:cd17946 160 KGH--FAE-LEKILellnkdRAGKKRKRQTFVFSATLTLDHQLPLKLN 204
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
177-376 |
7.63e-33 |
|
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: 124.58 E-value: 7.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 177 LLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL----KQPTnkgfrALVISPTRELASQIH 252
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCltehRNPS-----ALILTPTRELAVQIE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 253 RELIKISEGTgfrIHMIHKAAIAAKKFGP---KSSKKFDILVTTPNRLIYLLKQEppGIDLTSVEWLVVDESDKLFedgK 329
Cdd:cd17962 76 DQAKELMKGL---PPMKTALLVGGLPLPPqlyRLQQGVKVIIATPGRLLDILKQS--SVELDNIKIVVVDEADTML---K 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16758984 330 TGFRDQLASIFLAcTSPKVRRAMFSATFAYDVEQWCKLNLDNIVSVS 376
Cdd:cd17962 148 MGFQQQVLDILEN-ISHDHQTILVSATIPRGIEQLAGQLLQNPVRIT 193
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
163-376 |
8.93e-33 |
|
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: 124.74 E-value: 8.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 163 TFQQLDqeykISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL---KQPtnkgFRAL 239
Cdd:cd17954 1 TFKELG----VCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALlenPQR----FFAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 240 VISPTRELASQIHRELIKISEGTGFRIHMI------HKAAIAAkkfgpksSKKFDILVTTPNRLIYLLKQEpPGIDLTSV 313
Cdd:cd17954 73 VLAPTRELAQQISEQFEALGSSIGLKSAVLvggmdmMAQAIAL-------AKKPHVIVATPGRLVDHLENT-KGFSLKSL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16758984 314 EWLVVDESDKLFEdgkTGFRDQLASIFLacTSPKVRRAM-FSATFAYDVEQWCKLNLDNIVSVS 376
Cdd:cd17954 145 KFLVMDEADRLLN---MDFEPEIDKILK--VIPRERTTYlFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
169-361 |
2.05e-32 |
|
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: 123.56 E-value: 2.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 169 QEYKISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLkQPTNKGFRALVISPTRELA 248
Cdd:cd17940 2 EDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI-DPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 249 SQIHRELIKISEGTGfrihmihkaAIAAKKFGPKSSK--------KFDILVTTPNRLIYLLKQEPpgIDLTSVEWLVVDE 320
Cdd:cd17940 81 LQTSQVCKELGKHMG---------VKVMVTTGGTSLRddimrlyqTVHVLVGTPGRILDLAKKGV--ADLSHCKTLVLDE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16758984 321 SDKLFEDGKTGFRDQLASIFlactsPKVRRAM-FSATFAYDV 361
Cdd:cd17940 150 ADKLLSQDFQPIIEKILNFL-----PKERQILlFSATFPLTV 186
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
169-356 |
2.69e-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: 120.79 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 169 QEYKISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQ-PTnkGFRALVISPTREL 247
Cdd:cd17955 2 EDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEdPY--GIFALVLTPTREL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 248 ASQIHRELIKISEGTGFR-------IHMIHKAAIAAKKfgPKsskkfdILVTTPNRLIYLLKQEPPGI-DLTSVEWLVVD 319
Cdd:cd17955 80 AYQIAEQFRALGAPLGLRccvivggMDMVKQALELSKR--PH------IVVATPGRLADHLRSSDDTTkVLSRVKFLVLD 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 16758984 320 ESDKLFEDgktGFRDQLASIFLACtsPKVRR-AMFSAT 356
Cdd:cd17955 152 EADRLLTG---SFEDDLATILSAL--PPKRQtLLFSAT 184
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
177-363 |
8.81e-30 |
|
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: 116.41 E-value: 8.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 177 LLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL-KQPTNKGFR----ALVISPTRELASQI 251
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLdLQPIPREQRngpgVLVLTPTRELALQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 252 HRELIKISEgTGFRIHMIHKAAIAAKKFgPKSSKKFDILVTTPNRLIYLlkQEPPGIDLTSVEWLVVDESDKLFEdgkTG 331
Cdd:cd17958 81 EAECSKYSY-KGLKSVCVYGGGNRNEQI-EDLSKGVDIIIATPGRLNDL--QMNNVINLKSITYLVLDEADRMLD---MG 153
|
170 180 190
....*....|....*....|....*....|..
gi 16758984 332 FRDQLASIFLAcTSPKVRRAMFSATFAYDVEQ 363
Cdd:cd17958 154 FEPQIRKILLD-IRPDRQTIMTSATWPDGVRR 184
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
177-363 |
1.93e-29 |
|
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: 115.16 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 177 LLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLK-QP---TNKGFRALVISPTRELASQIH 252
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIVHINaQPpleRGDGPIVLVLAPTRELAQQIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 253 RELIKISEGTGFRIHMIHKAAiaakkfgPKSSKKFD------ILVTTPNRLIYLLKQEPpgIDLTSVEWLVVDESDKLFE 326
Cdd:cd17966 81 QEANKFGGSSRLRNTCVYGGA-------PKGPQIRDlrrgveICIATPGRLIDFLDQGK--TNLRRVTYLVLDEADRMLD 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 16758984 327 dgkTGFRDQLASIfLACTSPKVRRAMFSATFAYDVEQ 363
Cdd:cd17966 152 ---MGFEPQIRKI-VDQIRPDRQTLMWSATWPKEVRR 184
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
178-369 |
1.31e-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: 112.84 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 178 LQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIP---ILMQLK-QPTNkGFRALVISPTRELASQIH- 252
Cdd:cd17942 2 LKAIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPaieLLYKLKfKPRN-GTGVIIISPTRELALQIYg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 253 --RELIKISEGT-GFRIHMIHKAAIAAkkfgpKSSKKFDILVTTPNRLIYLLkQEPPGIDLTSVEWLVVDESDKLFEdgk 329
Cdd:cd17942 81 vaKELLKYHSQTfGIVIGGANRKAEAE-----KLGKGVNILVATPGRLLDHL-QNTKGFLYKNLQCLIIDEADRILE--- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16758984 330 TGFRDQLASIfLACTsPKVRRAM-FSATFAYDVEQWCKLNL 369
Cdd:cd17942 152 IGFEEEMRQI-IKLL-PKRRQTMlFSATQTRKVEDLARISL 190
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
175-365 |
1.99e-28 |
|
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: 112.41 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 175 PRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILmQLkqptnkgFRALVISPTRELASQIHRE 254
Cdd:cd17938 8 PELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-QI-------VVALILEPSRELAEQTYNC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 255 LIKisegtgFRIHM-----IHKAAIAAKKFGPKSS---KKFDILVTTPNRLIYLLKQEPpgIDLTSVEWLVVDESDKLFE 326
Cdd:cd17938 80 IEN------FKKYLdnpklRVALLIGGVKAREQLKrleSGVDIVVGTPGRLEDLIKTGK--LDLSSVRFFVLDEADRLLS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16758984 327 DGKTGFRDQLASIFLACTSPKVRRAM--FSATF-AYDVEQWC 365
Cdd:cd17938 152 QGNLETINRIYNRIPKITSDGKRLQVivCSATLhSFEVKKLA 193
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
169-366 |
3.94e-28 |
|
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: 112.05 E-value: 3.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 169 QEYKISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQPTNKgFRALVISPTRELA 248
Cdd:cd17950 5 RDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQ-VSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 249 SQIHRELIKISE-------GTGFRIHMIHKAAIAAKKFGPksskkfDILVTTPNRLIYLLKQEppGIDLTSVEWLVVDES 321
Cdd:cd17950 84 FQISNEYERFSKympnvktAVFFGGVPIKKDIEVLKNKCP------HIVVGTPGRILALVREK--KLKLSHVKHFVLDEC 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16758984 322 DKLFEDGKTgfRDQLASIFLACTSPKvRRAMFSATFAYDVEQWCK 366
Cdd:cd17950 156 DKMLEQLDM--RRDVQEIFRATPHDK-QVMMFSATLSKEIRPVCK 197
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
125-378 |
1.17e-27 |
|
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: 112.41 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 125 EKKLTSEKLE--HLRKEKINFFRNKHKIHVQGTDLPDPIATFQQLDqeykiSPRLLQNIL-DAGFQVPTPIQMQAIPVML 201
Cdd:cd18050 23 EKNFYVEHPEvaRMTQYDVEELRRKKEITIRGVGCPKPVFAFHQAN-----FPQYVMDVLlDQNFKEPTPIQCQGFPLAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 202 HGRELLASAPTGSGKTLAFSIPILMQLK-QP---TNKGFRALVISPTRELASQIHRELIKISEGTGFRIHMIHKAAIAak 277
Cdd:cd18050 98 SGRDMVGIAQTGSGKTLAYLLPAIVHINhQPyleRGDGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPK-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 278 kfGPKS---SKKFDILVTTPNRLIYLLkqEPPGIDLTSVEWLVVDESDKLFEdgkTGFRDQLASIfLACTSPKVRRAMFS 354
Cdd:cd18050 176 --GPQIrdlERGVEICIATPGRLIDFL--EAGKTNLRRCTYLVLDEADRMLD---MGFEPQIRKI-VDQIRPDRQTLMWS 247
|
250 260
....*....|....*....|....
gi 16758984 355 ATFAYDVEQWCKLNLDNIVSVSIG 378
Cdd:cd18050 248 ATWPKEVRQLAEDFLRDYVQINIG 271
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
185-376 |
1.82e-27 |
|
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: 109.98 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 185 GFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL-KQPT----NKGFRALVISPTRELASQIHRELIKIs 259
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlSLEPrvdrSDGTLALVLVPTRELALQIYEVLEKL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 260 egtGFRIHMIHKAAIAA--KKFGPKSS--KKFDILVTTPNRLIYLLK--QEppgIDLTSVEWLVVDESDKLFEdgkTGFR 333
Cdd:cd17949 89 ---LKPFHWIVPGYLIGgeKRKSEKARlrKGVNILIATPGRLLDHLKntQS---FDVSNLRWLVLDEADRLLD---MGFE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16758984 334 DQLASIF----------LACTSPKVRR--AMFSATFAYDVEQWCKLNLDNIVSVS 376
Cdd:cd17949 160 KDITKILellddkrskaGGEKSKPSRRqtVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
427-508 |
2.06e-27 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 105.37 E-value: 2.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 427 KELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGR 506
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 16758984 507 AG 508
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
139-379 |
1.30e-26 |
|
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: 108.56 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 139 EKINFFRNKHKIHVQGTDLPDPIATFQqldqEYKISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTL 218
Cdd:cd18049 1 QEVEQYRRSKEITVRGHNCPKPVLNFY----EANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 219 AFSIPILMQLK-QP---TNKGFRALVISPTRELASQIHRELIKISEGTGFRIHMIHKAAIAakkfGPKS---SKKFDILV 291
Cdd:cd18049 77 SYLLPAIVHINhQPfleRGDGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPK----GPQIrdlERGVEICI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 292 TTPNRLIYLLkqEPPGIDLTSVEWLVVDESDKLFEdgkTGFRDQLASIfLACTSPKVRRAMFSATFAYDVEQWCKLNLDN 371
Cdd:cd18049 153 ATPGRLIDFL--EAGKTNLRRCTYLVLDEADRMLD---MGFEPQIRKI-VDQIRPDRQTLMWSATWPKEVRQLAEDFLKD 226
|
....*...
gi 16758984 372 IVSVSIGA 379
Cdd:cd18049 227 YIHINIGA 234
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
170-373 |
2.87e-26 |
|
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: 106.25 E-value: 2.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 170 EYKISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLkQPTNKGFRALVISPTRELAS 249
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRI-DTTVRETQALVLAPTRELAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 250 QIHRELIKISEGTGFRIH-MIHKAAIAAKKFgpKSSKKFDILVTTPNRLIYLLKQEppGIDLTSVEWLVVDESDKLFedg 328
Cdd:cd17939 80 QIQKVVKALGDYMGVKVHaCIGGTSVREDRR--KLQYGPHIVVGTPGRVFDMLQRR--SLRTDKIKMFVLDEADEML--- 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16758984 329 KTGFRDQLASIFLACTsPKVRRAMFSATFAYDVEQWCKLNLDNIV 373
Cdd:cd17939 153 SRGFKDQIYDIFQFLP-PETQVVLFSATMPHEVLEVTKKFMRDPV 196
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
173-362 |
4.02e-26 |
|
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: 105.74 E-value: 4.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 173 ISPRLLQNILDAGFQVPTPIQMQAIPVMLHG--RELLASAPTGSGKTLAFSIPILMQLkQPTNKGFRALVISPTRELASQ 250
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-DPTLKSPQALCLAPTRELARQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 251 IHRELIKISEGTGFRIHmihkAAIAAKKFGPKSSKKFDILVTTPNRLIYLLKQEppGIDLTSVEWLVVDESDKLFEDGkt 330
Cdd:cd17963 80 IGEVVEKMGKFTGVKVA----LAVPGNDVPRGKKITAQIVIGTPGTVLDWLKKR--QLDLKKIKILVLDEADVMLDTQ-- 151
|
170 180 190
....*....|....*....|....*....|....
gi 16758984 331 GFRDQLASI--FLactSPKVRRAMFSATFAYDVE 362
Cdd:cd17963 152 GHGDQSIRIkrML---PRNCQILLFSATFPDSVR 182
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
177-363 |
2.66e-25 |
|
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: 104.37 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 177 LLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQ-LKQPTNKGF-----RALVISPTRELASQ 250
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRlLRYKLLAEGpfnapRGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 251 IHRELIKISEGTGFRIHMIH----KAAIAAKKFGpksskKFDILVTTPNRLIYLLKQEPpgIDLTSVEWLVVDESDKLFE 326
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITggrtKRQIRNPHFE-----EVDILVATPGALSKLLTSRI--YSLEQLRHLVLDEADTLLD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16758984 327 DGKTGF------RDQLASIFLACT---SPKVRRAMFSATFAYDVEQ 363
Cdd:cd17948 154 DSFNEKlshflrRFPLASRRSENTdglDPGTQLVLVSATMPSGVGE 199
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
177-357 |
3.91e-25 |
|
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: 102.73 E-value: 3.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 177 LLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKqPTNKGFRALVISPTRELASQIHRELI 256
Cdd:cd17943 1 VLEGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLD-LERRHPQVLILAPTREIAVQIHDVFK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 257 KISE-GTGFRIH-MIHKAAIAAKKfgpKSSKKFDILVTTPNRLIYLLKQEppGIDLTSVEWLVVDESDKLFEDgktGFRD 334
Cdd:cd17943 80 KIGKkLEGLKCEvFIGGTPVKEDK---KKLKGCHIAVGTPGRIKQLIELG--ALNVSHVRLFVLDEADKLMEG---SFQK 151
|
170 180
....*....|....*....|....
gi 16758984 335 QLASIFLACtsPKVRR-AMFSATF 357
Cdd:cd17943 152 DVNWIFSSL--PKNKQvIAFSATY 173
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
177-356 |
3.26e-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: 3.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 177 LLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILM-----QLKQP--TNKGFRALVISPTRELAS 249
Cdd:cd17951 1 ILKGLKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMfaleqEKKLPfiKGEGPYGLIVCPSRELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 250 QIHrELI-----KISEGTGFRIH-MIHKAAIAAKKFGPKSSKKFDILVTTPNRLIYLLKQEPpgIDLTSVEWLVVDESDK 323
Cdd:cd17951 81 QTH-EVIeyyckALQEGGYPQLRcLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKK--INLDICRYLCLDEADR 157
|
170 180 190
....*....|....*....|....*....|...
gi 16758984 324 LFEdgkTGFRDQLASIFLACTSPKvRRAMFSAT 356
Cdd:cd17951 158 MID---MGFEEDIRTIFSYFKGQR-QTLLFSAT 186
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
202-530 |
2.16e-23 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 104.34 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 202 HGRELLASAPTGSGKTLAFSIpILMQLKQPTnkgfRALVISPTRELASQIHRELIKISEGTGFrihmihkaaiaakkFGP 281
Cdd:COG1061 99 GGGRGLVVAPTGTGKTVLALA-LAAELLRGK----RVLVLVPRRELLEQWAEELRRFLGDPLA--------------GGG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 282 KSSKKFDILVTTPNRLIYLLKQE--PPGIDLtsvewLVVDE----SDKLFEdgktgfrdQLASIFlactsPKVRRAMFSA 355
Cdd:COG1061 160 KKDSDAPITVATYQSLARRAHLDelGDRFGL-----VIIDEahhaGAPSYR--------RILEAF-----PAAYRLGLTA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 356 T-FAYDVEQWCKLNLDNIV----------------------SVSIGARNSAVETVEQEL--LFVGSETGKLLAMRELVKK 410
Cdd:COG1061 222 TpFRSDGREILLFLFDGIVyeyslkeaiedgylappeyygiRVDLTDERAEYDALSERLreALAADAERKDKILRELLRE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 411 -GFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYD 489
Cdd:COG1061 302 hPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVAILLR 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 16758984 490 fPTSS-VEYIHRIGRTGRAGNRGKAVTFFT--EDDKPLLRSVAN 530
Cdd:COG1061 382 -PTGSpREFIQRLGRGLRPAPGKEDALVYDfvGNDVPVLEELAK 424
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
173-361 |
2.32e-21 |
|
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: 92.51 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 173 ISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLkQPTNKGFRALVISPTRELASQIH 252
Cdd:cd18046 6 LKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQI-DTSLKATQALVLAPTRELAQQIQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 253 RELIKISEGTGFRIHmihkAAIAAKKFGPKSSKKFD---ILVTTPNRLIYLLKQEppGIDLTSVEWLVVDESDKLFEdgk 329
Cdd:cd18046 85 KVVMALGDYMGIKCH----ACIGGTSVRDDAQKLQAgphIVVGTPGRVFDMINRR--YLRTDYIKMFVLDEADEMLS--- 155
|
170 180 190
....*....|....*....|....*....|..
gi 16758984 330 TGFRDQLASIFlACTSPKVRRAMFSATFAYDV 361
Cdd:cd18046 156 RGFKDQIYDIF-QKLPPDTQVVLLSATMPNDV 186
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
188-327 |
1.24e-20 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 91.67 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 188 VPTPIQMQAIPVMLHGR----------------ELLASAPTGSGKTLAFSIPILMQLKQ----------------PTNKG 235
Cdd:cd17965 30 KPSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKRqeqepfeeaeeeyesaKDTGR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 236 FRALVISPTRELASQIHRELIKISEGTGFRIHMIhKAAIAA--KKFGPKSSKKFDILVTTPNRLIYLLKQEPPgiDLTSV 313
Cdd:cd17965 110 PRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTF-SSGFGPsyQRLQLAFKGRIDILVTTPGKLASLAKSRPK--ILSRV 186
|
170
....*....|....
gi 16758984 314 EWLVVDESDKLFED 327
Cdd:cd17965 187 THLVVDEADTLFDR 200
|
|
| DEXH_lig_assoc |
TIGR04121 |
DEXH box helicase, DNA ligase-associated; Members of this protein family are DEAD/DEAH box ... |
189-516 |
6.94e-20 |
|
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: 94.16 E-value: 6.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 189 PTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL---KQPTNKGFRALVISPTRELASQIHRELIKISEGTG-- 263
Cdd:TIGR04121 14 PRPFQLEMWAAALEGRSGLLIAPTGSGKTLAGFLPSLIDLagpEAPKEKGLHTLYITPLRALAVDIARNLQAPIEELGlp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 264 FRIHM------IHKAAiAAKKFGPksskkfDILVTTPNRLIYLLKQEPPGIDLTSVEWLVVDESDKLFEdGKTGFRDQLA 337
Cdd:TIGR04121 94 IRVETrtgdtsSSERA-RQRKKPP------DILLTTPESLALLLSYPDAARLFKDLRCVVVDEWHELAG-SKRGDQLELA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 338 SIFLACTSPKVRRAMFSATFAyDVEQ---WCkLNLDNIVSVSIGA---RNSAVETV--EQELLFVGSETGKLLAMRELVK 409
Cdd:TIGR04121 166 LARLRRLAPGLRRWGLSATIG-NLEEarrVL-LGVGGAPAVLVRGklpKAIEVISLlpESEERFPWAGHLGLRALPEVYA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 410 K-GFNPPVLVFVQSIERAKELFHELIYegINVD---VI---HAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGV 482
Cdd:TIGR04121 244 EiDQARTTLVFTNTRSQAELWFQALWE--ANPEfalPIalhHGSLDREQRRWVEAAMAAGRLRAVVCTSSLDLGVDFGPV 321
|
330 340 350
....*....|....*....|....*....|....
gi 16758984 483 NLVINYDFPTSSVEYIHRIGRTGRAGNRGKAVTF 516
Cdd:TIGR04121 322 DLVIQIGSPKGVARLLQRAGRSNHRPGEPSRALL 355
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
177-361 |
7.76e-20 |
|
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: 87.91 E-value: 7.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 177 LLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILmQLKQPTNKGFRALVISPTRELASQIHRELI 256
Cdd:cd18045 10 LLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVL-QCLDIQVRETQALILSPTRELAVQIQKVLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 257 KISEGTGFRIHmihkAAIAAKKFGPKSSK---KFDILVTTPNRLIYLLKQEppGIDLTSVEWLVVDESDKLFEDgktGFR 333
Cdd:cd18045 89 ALGDYMNVQCH----ACIGGTSVGDDIRKldyGQHIVSGTPGRVFDMIRRR--SLRTRHIKMLVLDEADEMLNK---GFK 159
|
170 180
....*....|....*....|....*...
gi 16758984 334 DQLASIFlACTSPKVRRAMFSATFAYDV 361
Cdd:cd18045 160 EQIYDVY-RYLPPATQVVLVSATLPQDI 186
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
190-508 |
9.78e-19 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 89.57 E-value: 9.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 190 TPIQMQAIP-VMLHGRELLASAPTGSGKTLAFSIPILMQLkqptNKGFRALVISPTRELASQIHRELIKISEGTGFRIhm 268
Cdd:COG1204 24 YPPQAEALEaGLLEGKNLVVSAPTASGKTLIAELAILKAL----LNGGKALYIVPLRALASEKYREFKRDFEELGIKV-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 269 ihKAAIAAKKFGPKSSKKFDILVTTPNRLIYLLKQEPPGIDltSVEWLVVDESDKLfEDGKTGFRDQLASIFLACTSPKV 348
Cdd:COG1204 98 --GVSTGDYDSDDEWLGRYDILVATPEKLDSLLRNGPSWLR--DVDLVVVDEAHLI-DDESRGPTLEVLLARLRRLNPEA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 349 RRAMFSATF--AYDVEQWcklnLDNIVsvsigarnsaVET----VEQELLFV---------GSETGKL----LAMRELvk 409
Cdd:COG1204 173 QIVALSATIgnAEEIAEW----LDAEL----------VKSdwrpVPLNEGVLydgvlrfddGSRRSKDptlaLALDLL-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 410 kGFNPPVLVFVQSIERA-----------------------KELFHELIYEGINVDVI--------------HAERTQQQR 452
Cdd:COG1204 237 -EEGGQVLVFVSSRRDAeslakkladelkrrltpeereelEELAEELLEVSEETHTNekladclekgvafhHAGLPSELR 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758984 453 DNTVHSFRAGKIWVLICTALLArgidfKGVNL----VI--------NYDFPTSsvEYIHRIGRTGRAG 508
Cdd:COG1204 316 RLVEDAFREGLIKVLVATPTLA-----AGVNLparrVIirdtkrggMVPIPVL--EFKQMAGRAGRPG 376
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
203-356 |
4.97e-18 |
|
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: 81.48 E-value: 4.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 203 GRELLASAPTGSGKTLAFSIPILMQLKQPTNKGFRALVISPTRELASQIHRELIKISEGTGFRIHMIH---------KAA 273
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLEIPVAVrhgdtsqseKAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 274 IAAKkfgPKsskkfDILVTTPNRLIYLLKQEPPGIDLTSVEWLVVDESDKLFeDGKTGfrDQLASI---FLACTSPKVRR 350
Cdd:cd17922 81 QLKN---PP-----GILITTPESLELLLVNKKLRELFAGLRYVVVDEIHALL-GSKRG--VQLELLlerLRKLTGRPLRR 149
|
....*.
gi 16758984 351 AMFSAT 356
Cdd:cd17922 150 IGLSAT 155
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
186-505 |
2.46e-17 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 85.92 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 186 FQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL-----KQPTNKGFRALVISPTRELASQIHRELIK--- 257
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDELarrprPGELPDGLRVLYISPLKALANDIERNLRAple 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 258 -ISEGTGFRIHMIH------------KAAIAAKKfgPksskkfDILVTTPNRLiYLLkqeppgidLTS---------VEW 315
Cdd:COG1201 102 eIGEAAGLPLPEIRvgvrtgdtpaseRQRQRRRP--P------HILITTPESL-ALL--------LTSpdarellrgVRT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 316 LVVDE-----SDKlfedgktgfR-DQLAsifLA-------CTSPkVRRAMFSATFA-----------YDVEQWCKlnldn 371
Cdd:COG1201 165 VIVDEihalaGSK---------RgVHLA---LSlerlralAPRP-LQRIGLSATVGpleevarflvgYEDPRPVT----- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 372 IVSVSIGARnsavetVEQELLFVGSETGKLLAMRELVKKGFNPPV----------LVFV----QSiERakeLFHEL--IY 435
Cdd:COG1201 227 IVDAGAGKK------PDLEVLVPVEDLIERFPWAGHLWPHLYPRVldlieahrttLVFTntrsQA-ER---LFQRLneLN 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16758984 436 EGINVDV-IH-----AErtqqQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTG 505
Cdd:COG1201 297 PEDALPIaAHhgslsRE----QRLEVEEALKAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAG 368
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
190-364 |
2.80e-17 |
|
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: 80.00 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 190 TPIQMQAI-PVMLHGRELLASAPTGSGKTLAFSIPILMQLKQptnKGFRALVISPTRELASQIHRELIKISEGTGFRIHM 268
Cdd:cd17921 3 NPIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALAT---SGGKAVYIAPTRALVNQKEADLRERFGPLGKNVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 269 IhkaaIAAKKFGPKSSKKFDILVTTPNRL-IYLLKQEPPGIDLtsVEWLVVDESdKLFEDGKTGFRDQLASIFLACTSPK 347
Cdd:cd17921 80 L----TGDPSVNKLLLAEADILVATPEKLdLLLRNGGERLIQD--VRLVVVDEA-HLIGDGERGVVLELLLSRLLRINKN 152
|
170
....*....|....*....
gi 16758984 348 VRRAMFSATF--AYDVEQW 364
Cdd:cd17921 153 ARFVGLSATLpnAEDLAEW 171
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
173-524 |
4.03e-15 |
|
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: 78.72 E-value: 4.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 173 ISPRLLQNILDAGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQptNKGFRALVISPTRELASQIH 252
Cdd:COG1205 41 LPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLE--DPGATALYLYPTKALARDQL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 253 RELIKISEGTGFRIHmihkaaiAAKKFG--PKSSKKF-----DILVTTPNRLIY-LLKQEPPGID-LTSVEWLVVDES-- 321
Cdd:COG1205 119 RRLRELAEALGLGVR-------VATYDGdtPPEERRWirehpDIVLTNPDMLHYgLLPHHTRWARfFRNLRYVVIDEAht 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 322 -DKLFedgktG------FR------DQLAS--IFLACtspkvrramfSATFAYDVEQWCKL------------------- 367
Cdd:COG1205 192 yRGVF-----GshvanvLRrlrricRHYGSdpQFILA----------SATIGNPAEHAERLtgrpvtvvdedgsprgert 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 368 -NLDNIVSVSIGARNSAVetveqellfvgSETGKLLAmrELVKKGFNppVLVFVQSI-------ERAKELFHELIYeGIN 439
Cdd:COG1205 257 fVLWNPPLVDDGIRRSAL-----------AEAARLLA--DLVREGLR--TLVFTRSRrgaellaRYARRALREPDL-ADR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 440 VDVIHAERTQQQRDNTVHSFRAGKIWVLICT-AL-LarGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNRGKAVTFF 517
Cdd:COG1205 321 VAAYRAGYLPEERREIERGLRSGELLGVVSTnALeL--GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLVVLVA 398
|
....*..
gi 16758984 518 TEDdkPL 524
Cdd:COG1205 399 GDD--PL 403
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
191-361 |
5.13e-15 |
|
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: 74.11 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 191 PIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLK---QPTNKGF--RALVISPTRELASQIHRELIKISEG---T 262
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQedqQPRKRGRapKVLVLAPTRELANQVTKDFKDITRKlsvA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 263 GFRIHMIHKAAIAAKKFGpksskkFDILVTTPNRLIYLLKQEPpgIDLTSVEWLVVDESDKLFEdgkTGFRDQLASI--- 339
Cdd:cd17944 95 CFYGGTPYQQQIFAIRNG------IDILVGTPGRIKDHLQNGR--LDLTKLKHVVLDEVDQMLD---MGFAEQVEEIlsv 163
|
170 180
....*....|....*....|....*.
gi 16758984 340 -FLACTSPKVRRAMFSAT---FAYDV 361
Cdd:cd17944 164 sYKKDSEDNPQTLLFSATcpdWVYNV 189
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
203-356 |
7.81e-15 |
|
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: 72.05 E-value: 7.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 203 GRELLASAPTGSGKTLAFSIPILMQLKQptnKGFRALVISPTRELASQIHRELIKISeGTGFRIHMIHkaaiAAKKFGPK 282
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLK---KGKKVLVLVPTKALALQTAERLRELF-GPGIRVAVLV----GGSSAEER 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758984 283 SSKKF---DILVTTPNRlIYLLKQEPPGIDLTSVEWLVVDESDKLfeDGKTGFRDQLASIFLACTSPKVRRAMFSAT 356
Cdd:cd00046 73 EKNKLgdaDIIIATPDM-LLNLLLREDRLFLKDLKLIIVDEAHAL--LIDSRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| PRK01172 |
PRK01172 |
ATP-dependent DNA helicase; |
193-508 |
5.28e-14 |
|
ATP-dependent DNA helicase;
Pssm-ID: 100801 [Multi-domain] Cd Length: 674 Bit Score: 75.30 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 193 QMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKqptnKGFRALVISPTRELASQIHRELIKISEgTGFRIHMihka 272
Cdd:PRK01172 27 QRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFL----AGLKSIYIVPLRSLAMEKYEELSRLRS-LGMRVKI---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 273 AIAAKKFGPKSSKKFDILVTTPNRLIYLLKQEPPGIDltSVEWLVVDESDKLFEDGKTGFRDQLASIfLACTSPKVRRAM 352
Cdd:PRK01172 98 SIGDYDDPPDFIKRYDVVILTSEKADSLIHHDPYIIN--DVGLIVADEIHIIGDEDRGPTLETVLSS-ARYVNPDARILA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 353 FSATF--AYDVEQWckLNLDNIVSvSIGARNSAVETVEQELLFVGSETGKLLAMRELVKKGFNP--PVLVFVQSIERAK- 427
Cdd:PRK01172 175 LSATVsnANELAQW--LNASLIKS-NFRPVPLKLGILYRKRLILDGYERSQVDINSLIKETVNDggQVLVFVSSRKNAEd 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 428 --------------------------ELFHELIYEGINVDviHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKG 481
Cdd:PRK01172 252 yaemliqhfpefndfkvssennnvydDSLNEMLPHGVAFH--HAGLSNEQRRFIEEMFRNRYIKVIVATPTLAAGVNLPA 329
|
330 340 350
....*....|....*....|....*....|....*.
gi 16758984 482 vNLVINYDF---------PTSSVEYIHRIGRTGRAG 508
Cdd:PRK01172 330 -RLVIVRDItrygnggirYLSNMEIKQMIGRAGRPG 364
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
148-357 |
1.13e-13 |
|
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: 70.82 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 148 HKIHVQGTDLPDPIATFQQLdQEYKISPRLLQNILDAGFQVPTPIQMQAIPVMLHG--RELLASAPTGSGKTLAFSIPIL 225
Cdd:cd18048 1 HRVEVLQRDPTSPLFSVKSF-EELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAML 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 226 MQLKqpTNKGF-RALVISPTRELASQIHR---ELIKISEGtgfrIHMIHkaAIAAKKFGPKSSKKFDILVTTPNRLI--- 298
Cdd:cd18048 80 SRVD--ALKLYpQCLCLSPTFELALQTGKvveEMGKFCVG----IQVIY--AIRGNRPGKGTDIEAQIVIGTPGTVLdwc 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758984 299 YLLKQeppgIDLTSVEWLVVDESDKLFEdgKTGFRDQlasiflactSPKVRRAM--------FSATF 357
Cdd:cd18048 152 FKLRL----IDVTNISVFVLDEADVMIN--VQGHSDH---------SVRVKRSMpkecqmllFSATF 203
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
400-520 |
1.85e-13 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 73.61 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 400 KLLAMRELVKK--GFNPP--VLVFVQSIERAKELFHELIYEGINVD--VIHAER------TQQQRDNTVHSFRAGKIWVL 467
Cdd:COG1111 336 KLSKLREILKEqlGTNPDsrIIVFTQYRDTAEMIVEFLSEPGIKAGrfVGQASKegdkglTQKEQIEILERFRAGEFNVL 415
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 16758984 468 ICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRaGNRGKAVTFFTED 520
Cdd:COG1111 416 VATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQRKGRTGR-KREGRVVVLIAKG 467
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
169-357 |
4.87e-13 |
|
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350805 [Multi-domain] Cd Length: 205 Bit Score: 68.21 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 169 QEYKISPRLLQNILDAGFQVPTPIQMQAIPVMLHG--RELLASAPTGSGKTLAFSIPILMQLkQPTNKGFRALVISPTRE 246
Cdd:cd18047 4 EELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV-EPANKYPQCLCLSPTYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 247 LASQIHRELIKISEgtgFRIHMIHKAAIAAKKFGPKSSKKFDILVTTPNRLI-YLLKQEPpgIDLTSVEWLVVDESDKLF 325
Cdd:cd18047 83 LALQTGKVIEQMGK---FYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLdWCSKLKF--IDPKKIKVFVLDEADVMI 157
|
170 180 190
....*....|....*....|....*....|...
gi 16758984 326 edGKTGFRDQlaSIFLACTSPK-VRRAMFSATF 357
Cdd:cd18047 158 --ATQGHQDQ--SIRIQRMLPRnCQMLLFSATF 186
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
191-320 |
5.28e-12 |
|
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: 64.66 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 191 PIQMQAI-PVMLHGRELLASAPTGSGKTLAFSIPILMQLKqptnKGFRALVISPTRELASQIHRELiKISEGTGFRIhmi 269
Cdd:cd18028 4 PPQAEAVrAGLLKGENLLISIPTASGKTLIAEMAMVNTLL----EGGKALYLVPLRALASEKYEEF-KKLEEIGLKV--- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 16758984 270 hkaAIAAKKF--GPKSSKKFDILVTTPNRLIYLLKQEPPGIDLTSVewLVVDE 320
Cdd:cd18028 76 ---GISTGDYdeDDEWLGDYDIIVATYEKFDSLLRHSPSWLRDVGV--VVVDE 123
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
415-518 |
5.93e-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: 61.57 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 415 PVLVFVQSIERAKELFHELIyeginvdvihaertqqqrdntvhsfragkiwVLICTALLARGIDFKGVNLVINYDFPTSS 494
Cdd:cd18785 5 KIIVFTNSIEHAEEIASSLE-------------------------------ILVATNVLGEGIDVPSLDTVIFFDPPSSA 53
|
90 100
....*....|....*....|....
gi 16758984 495 VEYIHRIGRTGRAGNRGKAVTFFT 518
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 ... |
193-320 |
1.76e-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: 63.37 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 193 QMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQptNKGFRALVISPTRELA-SQIhRELIKISEGTGFRIHMihk 271
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLR--DPGSRALYLYPTKALAqDQL-RSLRELLEQLGLGIRV--- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 16758984 272 AAIAAKKfgPKSSKKF------DILVTTPNRLIYLL---KQEPPGIdLTSVEWLVVDE 320
Cdd:cd17923 79 ATYDGDT--PREERRAiirnppRILLTNPDMLHYALlphHDRWARF-LRNLRYVVLDE 133
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
193-526 |
2.77e-11 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 65.93 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 193 QMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMqLKQPTnkgfraLVISPtreLAS----QIhRELikisEGTGFRIHM 268
Cdd:COG0514 22 QEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALL-LPGLT------LVVSP---LIAlmkdQV-DAL----RAAGIRAAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 269 IH-----------KAAIAAKKFgpksskkfDILVTTPNRL-----IYLLKQEPpgIDLtsvewLVVDE----SD------ 322
Cdd:COG0514 87 LNsslsaeerrevLRALRAGEL--------KLLYVAPERLlnprfLELLRRLK--ISL-----FAIDEahciSQwghdfr 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 323 ----KLFEdgktgFRDQLASI-FLACT---SPKVRRamfsatfayDVEQwcKLNLDNIVSVSIG-ARNS---AVETVEQE 390
Cdd:COG0514 152 pdyrRLGE-----LRERLPNVpVLALTataTPRVRA---------DIAE--QLGLEDPRVFVGSfDRPNlrlEVVPKPPD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 391 llfvgsetGKLLAMRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICT 470
Cdd:COG0514 216 --------DKLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 16758984 471 ALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNRGKAVTFFTEDDKPLLR 526
Cdd:COG0514 288 IAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQR 343
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
186-320 |
5.84e-11 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 65.68 E-value: 5.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 186 FQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQL-----KQPTNKGFRALVISPTRELASQIHRELI---- 256
Cdd:PRK13767 30 FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELfrlgrEGELEDKVYCLYVSPLRALNNDIHRNLEeplt 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 257 ---KISEGTGFRIHMIhKAAIaakKFGPKSS--------KKFDILVTTPNRLIYLL-----KQEppgidLTSVEWLVVDE 320
Cdd:PRK13767 110 eirEIAKERGEELPEI-RVAI---RTGDTSSyekqkmlkKPPHILITTPESLAILLnspkfREK-----LRTVKWVIVDE 180
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
400-514 |
1.27e-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: 59.68 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 400 KLLAMRELVKKGF-------NPPVLVFVQSIERAKELFHELIYEGINVDVI----HAER------TQQQRDNTVHSFRAG 462
Cdd:cd18801 10 KLEKLEEIVKEHFkkkqegsDTRVIIFSEFRDSAEEIVNFLSKIRPGIRATrfigQASGksskgmSQKEQKEVIEQFRKG 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 16758984 463 KIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRaGNRGKAV 514
Cdd:cd18801 90 GYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVV 140
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
400-517 |
1.54e-10 |
|
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: 63.35 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 400 KLLA-MRELVKKGFnpPVLVFVQSIERAKELFHEL--IYEGINVDVIHAErtQQQRDNTVHSFRAGKIWVLICTALLARG 476
Cdd:COG4098 307 KLLKwLKKRLKEGR--QLLIFVPTIELLEQLVALLqkLFPEERIAGVHAE--DPERKEKVQAFRDGEIPILVTTTILERG 382
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 16758984 477 IDFKGVN-LVINYD---FPTSSVEYIHriGRTGRAGNR--GKaVTFF 517
Cdd:COG4098 383 VTFPNVDvAVLGADhpvFTEAALVQIA--GRVGRSADYptGE-VIFF 426
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
390-517 |
2.78e-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: 58.37 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 390 ELLFVGSETGKLLAMRELVKKGFNPPVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLIC 469
Cdd:cd18794 7 SVRPKDKKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVA 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 16758984 470 TALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNRGKAVTFF 517
Cdd:cd18794 87 TVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
393-524 |
1.62e-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: 56.58 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 393 FVGSETGKLLA---MRELVKKGFNPPVLVFVQSIERAKELFHELIYEgINVDVIHAERTQQQRDNTVHSFRAGKIWVLIC 469
Cdd:cd18810 5 YVMPYDDELIReaiERELLRGGQVFYVHNRIESIEKLATQLRQLVPE-ARIAIAHGQMTENELEEVMLEFAKGEYDILVC 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 16758984 470 TALLARGIDFKGVNLVINYDFPTSSVEYIHRI-GRTGRAGNRGKAVtFFTEDDKPL 524
Cdd:cd18810 84 TTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKERAYAY-FLYPDQKKL 138
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
400-520 |
2.98e-09 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 59.89 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 400 KLLAMRELVKK--GFNPP--VLVFVQSIERAKELFHELIYEGINvdvihAER-------------TQQQRDNTVHSFRAG 462
Cdd:PRK13766 348 KLEKLREIVKEqlGKNPDsrIIVFTQYRDTAEKIVDLLEKEGIK-----AVRfvgqaskdgdkgmSQKEQIEILDKFRAG 422
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 16758984 463 KIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRaGNRGKAVTFFTED 520
Cdd:PRK13766 423 EFNVLVSTSVAEEGLDIPSVDLVIFYEPVPSEIRSIQRKGRTGR-QEEGRVVVLIAKG 479
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
446-509 |
4.05e-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: 52.59 E-value: 4.05e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16758984 446 ERTQQQRdnTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRtGRAGN 509
Cdd:cd18802 75 TQRKQKE--TLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPN 135
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
416-510 |
4.36e-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: 52.65 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 416 VLVFVQSIERAKELFHEL------IYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYD 489
Cdd:cd18796 41 TLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIG 120
|
90 100
....*....|....*....|.
gi 16758984 490 FPTSSVEYIHRIGRTGRAGNR 510
Cdd:cd18796 121 SPKSVARLLQRLGRSGHRPGA 141
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
397-504 |
4.47e-08 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 56.00 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 397 ETGKLLAMRELVKKGFNP--PVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGK-IWV-LICTAL 472
Cdd:COG0553 531 RSAKLEALLELLEELLAEgeKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPVfLISLKA 610
|
90 100 110
....*....|....*....|....*....|....*...
gi 16758984 473 LARGIDFKGVNLVINYDFP-TSSVEY-----IHRIGRT 504
Cdd:COG0553 611 GGEGLNLTAADHVIHYDLWwNPAVEEqaidrAHRIGQT 648
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
399-502 |
5.62e-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: 51.71 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 399 GKLLAMRELVKKGFNPP--VLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAG-KIWV-LICTALLA 474
Cdd:cd18793 11 GKLEALLELLEELREPGekVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVfLLSTKAGG 90
|
90 100 110
....*....|....*....|....*....|....
gi 16758984 475 RGIDFKGVNLVINYDFP-TSSVEY-----IHRIG 502
Cdd:cd18793 91 VGLNLTAANRVILYDPWwNPAVEEqaidrAHRIG 124
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
400-514 |
1.64e-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: 51.01 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 400 KLLAMRELVKKGfnpPVLVFVQSieR------AKEL----FHeliyeginvdviHAERTQQQRDnTVHS-FRAGKIWVLI 468
Cdd:cd18795 33 VLLKIETVSEGK---PVLVFCSS--RkecektAKDLagiaFH------------HAGLTREDRE-LVEElFREGLIKVLV 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758984 469 CTALLArgidfKGVNL----VI----------NYDFPTSSvEYIHRIGRTGRAG--NRGKAV 514
Cdd:cd18795 95 ATSTLA-----AGVNLpartVIikgtqrydgkGYRELSPL-EYLQMIGRAGRPGfdTRGEAI 150
|
|
| PRK00254 |
PRK00254 |
ski2-like helicase; Provisional |
170-374 |
1.72e-07 |
|
ski2-like helicase; Provisional
Pssm-ID: 234702 [Multi-domain] Cd Length: 720 Bit Score: 54.44 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 170 EYKISPRLLQNILDAGFQVPTPIQMQAIPV-MLHGRELLASAPTGSGKTLAFSIPILMQLKQptnKGFRALVISPTRELA 248
Cdd:PRK00254 5 ELRVDERIKRVLKERGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLR---EGGKAVYLVPLKALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 249 SQIHRELiKISEGTGFRIHMIHkaaiaakkfGPKSSK-----KFDILVTTPNRLIYLLKQEPPGIDltSVEWLVVDESDK 323
Cdd:PRK00254 82 EEKYREF-KDWEKLGLRVAMTT---------GDYDSTdewlgKYDIIIATAEKFDSLLRHGSSWIK--DVKLVVADEIHL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16758984 324 LfedgktGFRDQLASI--FLACTSPKVRRAMFSATF--AYDVEQWckLNLDNIVS 374
Cdd:PRK00254 150 I------GSYDRGATLemILTHMLGRAQILGLSATVgnAEELAEW--LNAELVVS 196
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
191-320 |
1.95e-07 |
|
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: 50.77 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 191 PIQMQAIPVML---HGRELLASAPTGSGKTLaFSIPILMQLKQptnkgFRALVISPTRELASQIHRELIKISEGtgfriH 267
Cdd:cd17926 3 PYQEEALEAWLahkNNRRGILVLPTGSGKTL-TALALIAYLKE-----LRTLIVVPTDALLDQWKERFEDFLGD-----S 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 16758984 268 MIHKAAIAAKkfgpKSSKKFDILVTTPNRLIYLLKQEPPGIDLTSVewLVVDE 320
Cdd:cd17926 72 SIGLIGGGKK----KDFDDANVVVATYQSLSNLAEEEKDLFDQFGL--LIVDE 118
|
|
| DEXHc_POLQ-like |
cd18026 |
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ... |
198-356 |
2.86e-07 |
|
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: 51.45 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 198 PVMLHGRELLASAPTGSGKTLAFSipILMqLKQPTNKGFRALVISPTRELASQIHRELIKISEGTGFRI--HMIHKaaia 275
Cdd:cd18026 28 PGLLEGRNLVYSLPTSGGKTLVAE--ILM-LKRLLERRKKALFVLPYVSIVQEKVDALSPLFEELGFRVegYAGNK---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 276 aKKFGPKSSKKFDILVTTP-------NRLIYLLKQEPPGIdltsvewLVVDESDKLFEDGKTGFRDQLASIFLACTSPKV 348
Cdd:cd18026 101 -GRSPPKRRKSLSVAVCTIekanslvNSLIEEGRLDELGL-------VVVDELHMLGDGHRGALLELLLTKLLYAAQKNI 172
|
....*...
gi 16758984 349 RRAMFSAT 356
Cdd:cd18026 173 QIVGMSAT 180
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
192-254 |
8.23e-07 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 50.05 E-value: 8.23e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758984 192 IQMQAIPVMLHGRE-LLASAPTGSGKTLAFSIPILMQLKQPTNKG---FRALVISPTRELASQIHRE 254
Cdd:cd18023 5 IQSEVFPDLLYSDKnFVVSAPTGSGKTVLFELAILRLLKERNPLPwgnRKVVYIAPIKALCSEKYDD 71
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
420-529 |
6.52e-06 |
|
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: 46.49 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 420 VQSIERAKELFHELIYEgINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIH 499
Cdd:cd18792 44 LKSIEALAEELKELVPE-ARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLH 122
|
90 100 110
....*....|....*....|....*....|.
gi 16758984 500 RI-GRTGRAGNRGKAvtFFTEDDKPLLRSVA 529
Cdd:cd18792 123 QLrGRVGRGKHQSYC--YLLYPDPKKLTETA 151
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
396-510 |
9.14e-06 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 45.71 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 396 SETGKLLAmrELVKKGFNppVLVFVQS---IER-AKELFHELIYEGINVDVIHAER---TQQQRDNTVHSFRAGKIWVLI 468
Cdd:cd18797 22 REAARLFA--DLVRAGVK--TIVFCRSrklAELlLRYLKARLVEEGPLASKVASYRagyLAEDRREIEAELFNGELLGVV 97
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 16758984 469 CTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNR 510
Cdd:cd18797 98 ATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKD 139
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
185-243 |
1.07e-05 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 46.76 E-value: 1.07e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 16758984 185 GFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMqLKQPTnkgfraLVISP 243
Cdd:cd17920 9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALL-LDGVT------LVVSP 60
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
189-265 |
1.65e-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: 45.87 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 189 PTPIQMQAIPVMLHG------RELLASAPTGSGKTLAFSIPILMQLkqptNKGFRALVISPTRELASQIHREL------I 256
Cdd:cd17918 16 LTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAY----KNGKQVAILVPTEILAHQHYEEArkflpfI 91
|
....*....
gi 16758984 257 KISEGTGFR 265
Cdd:cd17918 92 NVELVTGGT 100
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
188-320 |
3.21e-05 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 45.16 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 188 VPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQPTNKGF--RALVISPTRELASQIHRELIKISEGtGFR 265
Cdd:cd18036 2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRSAGEkgRVVVLVNKVPLVEQQLEKFFKYFRK-GYK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 16758984 266 IHMIHKAAiAAKKFGPKSSKKFDILVTTPNRLIYLLK--QEPPGIDLTSVEWLVVDE 320
Cdd:cd18036 81 VTGLSGDS-SHKVSFGQIVKASDVIICTPQILINNLLsgREEERVYLSDFSLLIFDE 136
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
201-293 |
3.22e-05 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 45.01 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 201 LHGRELLASAPTGSGKT---LAFSIPIlmqlkqpTNKGFRALVISPTRELASQIHRELIKISEGTGFRIHMIHKAAIAAK 277
Cdd:cd17924 30 LRGKSFAIIAPTGVGKTtfgLATSLYL-------ASKGKRSYLIFPTKSLVKQAYERLSKYAEKAGVEVKILVYHSRLKK 102
|
90 100
....*....|....*....|.
gi 16758984 278 KFGPKSSKK-----FDILVTT 293
Cdd:cd17924 103 KEKEELLEKiekgdFDILVTT 123
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
176-320 |
3.42e-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: 44.94 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 176 RLLQNILdaGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQptnKGFRALVISPTREL-ASQIHRe 254
Cdd:cd18018 2 KLLRRVF--GHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRR---GPGLTLVVSPLIALmKDQVDA- 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758984 255 LIKISEGTgfRIHMIHKAAIAAKKFGPKSSKKFDILVTTPNRL-----IYLLKQEPPgIDLtsvewLVVDE 320
Cdd:cd18018 76 LPRAIKAA--ALNSSLTREERRRILEKLRAGEVKILYVSPERLvnesfRELLRQTPP-ISL-----LVVDE 138
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
210-270 |
4.37e-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: 46.13 E-value: 4.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16758984 210 APTGSGKTLAFSIPILMQLKqptnKGFRALVISPTRELASQIHRELIKisegTGFRIHMIH 270
Cdd:COG3505 6 GPTGSGKTVGLVIPNLTQLA----RGESVVVTDPKGDLAELTAGFRRR----AGYDVYVFD 58
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
417-503 |
4.80e-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: 42.93 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 417 LVFVQSIERAKELFHELIYEGINVDVIHAERTQQQR-DNTVHSFRAGKIW--VLICTALLARGIDFKGVNLVInYDFPT- 492
Cdd:cd18799 10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERgDEALILLFFGELKppILVTVDLLTTGVDIPEVDNVV-FLRPTe 88
|
90
....*....|.
gi 16758984 493 SSVEYIHRIGR 503
Cdd:cd18799 89 SRTLFLQMLGR 99
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
361-519 |
5.10e-05 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 43.78 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 361 VEQWCKLNLDNIVSVSIGARNSavetvEQELLFVGSeTGKLLAMRELVKKGFNP-PVLVFVQSIERAKElfhelIYEGIN 439
Cdd:cd18789 2 AEIRCPMTPEFYREYLGLGAHR-----KRRLLAAMN-PNKLRALEELLKRHEQGdKIIVFTDNVEALYR-----YAKRLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 440 VDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDF--KGVNLVINYDFpTSSVEYIHRIGRTGRAGNRGKAVTFF 517
Cdd:cd18789 71 KPFITGETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLpeANVAIQISGHG-GSRRQEAQRLGRILRPKKGGGKNAFF 149
|
..
gi 16758984 518 TE 519
Cdd:cd18789 150 YS 151
|
|
| PRK02362 |
PRK02362 |
ATP-dependent DNA helicase; |
191-320 |
7.74e-05 |
|
ATP-dependent DNA helicase;
Pssm-ID: 235032 [Multi-domain] Cd Length: 737 Bit Score: 45.72 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 191 PIQMQAIPV-MLHGRELLASAPTGSGKTLafsIPILMQLKQPTNKGfRALVISPTRELASQIHRELIKISEgTGFRIhmi 269
Cdd:PRK02362 26 PPQAEAVEAgLLDGKNLLAAIPTASGKTL---IAELAMLKAIARGG-KALYIVPLRALASEKFEEFERFEE-LGVRV--- 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 16758984 270 hkaAIAAKKFGPKSS--KKFDILVTTPNRLIYLLKQEPPGIDLTSVewLVVDE 320
Cdd:PRK02362 98 ---GISTGDYDSRDEwlGDNDIIVATSEKVDSLLRNGAPWLDDITC--VVVDE 145
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
415-528 |
8.36e-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: 44.54 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 415 PVLVFV----QSIERA-KELFHEliYEGINVDVIHAeRTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLV--IN 487
Cdd:cd18804 94 EDLVFKgigtERVEEElKTLFPE--ARIARIDRDTT-RKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLN 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 16758984 488 YDFPTSSVEY---------IHRI-GRTGRAGNRGKAV--TFFTEDdkPLLRSV 528
Cdd:cd18804 171 ADSGLNSPDFraserafqlLTQVsGRAGRGDKPGKVIiqTYNPEH--PLIQAA 221
|
|
| DEXHc_ASCC3_1 |
cd18020 |
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
192-327 |
9.46e-05 |
|
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: 43.96 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 192 IQMQAIPVMLHGRE-LLASAPTGSGKTLAFSIPILMQLKQPTNKG-------FRALVISPTRELASQIHREL-------- 255
Cdd:cd18020 5 IQSLVFPVAYKTNEnMLICAPTGAGKTNIAMLTILHEIRQHVNQGgvikkddFKIVYIAPMKALAAEMVEKFskrlaplg 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16758984 256 IKISEGTGfriHM-IHKAAIAAKKfgpksskkfdILVTTPNRLIYLLKQEPPGIDLTS-VEWLVVDESDKLFED 327
Cdd:cd18020 85 IKVKELTG---DMqLTKKEIAETQ----------IIVTTPEKWDVVTRKSSGDVALSQlVRLLIIDEVHLLHDD 145
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
161-526 |
2.86e-04 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 43.93 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 161 IATFQQLDQEyKISPRLLQNILdaGFQVPTPIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQlkqptnKGFrALV 240
Cdd:PRK11057 1 MAQAEVLNLE-SLAKQVLQETF--GYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVL------DGL-TLV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 241 ISPTREL-------------------ASQIHRELIKISEGTgfrihmihkaaiaakkfgpkSSKKFDILVTTPNRL---- 297
Cdd:PRK11057 71 VSPLISLmkdqvdqllangvaaaclnSTQTREQQLEVMAGC--------------------RTGQIKLLYIAPERLmmdn 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 298 -IYLLKQEPPGIdltsvewLVVDESDKLFEDGKTgFRDQLASI-----------FLACTspkvrrAMFSATFAYDVEQWC 365
Cdd:PRK11057 131 fLEHLAHWNPAL-------LAVDEAHCISQWGHD-FRPEYAALgqlrqrfptlpFMALT------ATADDTTRQDIVRLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 366 KLNlDNIVSVSI----GARNSAVET---VEQELLFVGSETGkllamrelvKKGfnppvLVFVQSIERAKELFHELIYEGI 438
Cdd:PRK11057 197 GLN-DPLIQISSfdrpNIRYTLVEKfkpLDQLMRYVQEQRG---------KSG-----IIYCNSRAKVEDTAARLQSRGI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 439 NVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTGRAGNRGKAVTFFT 518
Cdd:PRK11057 262 SAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYD 341
|
....*...
gi 16758984 519 EDDKPLLR 526
Cdd:PRK11057 342 PADMAWLR 349
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
191-243 |
3.34e-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: 42.35 E-value: 3.34e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 16758984 191 PIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMqlkqptNKGFrALVISP 243
Cdd:cd18015 21 PLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALC------SDGF-TLVVSP 66
|
|
| DEXHc_ASCC3_2 |
cd18022 |
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ... |
191-294 |
3.39e-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: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 191 PIQMQAIPVMLHGRE-LLASAPTGSGKTLAFSIPILMQLKQptNKGFRALVISPTRELAsqihRELI-----KISEGTGF 264
Cdd:cd18022 4 PIQTQVFHTLYHTDNnVLLGAPTGSGKTIAAELAMFRAFNK--YPGSKVVYIAPLKALV----RERVddwkkRFEEKLGK 77
|
90 100 110
....*....|....*....|....*....|
gi 16758984 265 RihMIHKAAIAAKKfgPKSSKKFDILVTTP 294
Cdd:cd18022 78 K--VVELTGDVTPD--MKALADADIIITTP 103
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
189-370 |
3.52e-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: 42.03 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 189 PTPIQMQAIPVMLHGRELLASAPTGSGKTLAfSIPILMQL--KQPTNKGFRALVISPTRELASQIHRELIKISEGTGFRI 266
Cdd:cd17927 3 PRNYQLELAQPALKGKNTIICLPTGSGKTFV-AVLICEHHlkKFPAGRKGKVVFLANKVPLVEQQKEVFRKHFERPGYKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 267 HMIhKAAIAAKKFGPKSSKKFDILVTTPNRLIYLLKQEPPgIDLTSVEWLVVDESD------------KLFEDGKTGFRD 334
Cdd:cd17927 82 TGL-SGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTI-VSLSDFSLLVFDECHnttknhpyneimFRYLDQKLGSSG 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 16758984 335 QLASIFLACTSPKVRRAmfsATFAYDVEQWCKL--NLD 370
Cdd:cd17927 160 PLPQILGLTASPGVGGA---KNTEEALEHICKLcaNLD 194
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
186-298 |
6.03e-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: 41.09 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 186 FQVPTPIQMQAIPVMLHGRE-LLASAPTGSGKTLAFSIPILMQLKQPTNKgfRALVISPTRELASQIHRELikisegtgf 264
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDnVFVGAPTGSGKTVCAELALLRHWRQNPKG--RAVYIAPMQELVDARYKDW--------- 69
|
90 100 110
....*....|....*....|....*....|....*..
gi 16758984 265 rihmihkaaiaAKKFGPKSSKKFDIL---VTTPNRLI 298
Cdd:cd18021 70 -----------RAKFGPLLGKKVVKLtgeTSTDLKLL 95
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
405-514 |
7.55e-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: 40.69 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 405 RELVKKGFNppVLVFVQSIERAKELFHELIYEGINVDVIHAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNL 484
Cdd:cd18790 21 RKRVARGER--VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSL 98
|
90 100 110
....*....|....*....|....*....|....*
gi 16758984 485 VINYD-----FPTSSVEYIHRIGRTGRAGNrGKAV 514
Cdd:cd18790 99 VAILDadkegFLRSETSLIQTIGRAARNVN-GKVI 132
|
|
| Dob10 |
COG4581 |
Superfamily II RNA helicase [Replication, recombination and repair]; |
191-258 |
9.56e-04 |
|
Superfamily II RNA helicase [Replication, recombination and repair];
Pssm-ID: 443638 [Multi-domain] Cd Length: 751 Bit Score: 42.23 E-value: 9.56e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16758984 191 PIQMQAIPVMLHGRELLASAPTGSGKTLAFSIPILMQLKQptnkGFRALVISPTRELASQIHRELIKI 258
Cdd:COG4581 28 PFQEEAILALEAGRSVLVAAPTGSGKTLVAEFAIFLALAR----GRRSFYTAPIKALSNQKFFDLVER 91
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
202-376 |
9.96e-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: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 202 HGRELLaSAPTGSGKTLAfsIPILMqLKQPTNKGFRALVISPTRELASQIHRELIK-----ISEGTGFRIHMIHkaaiaa 276
Cdd:cd17990 17 GGQVVL-EAPPGAGKTTR--VPLAL-LAELWIAGGKIIVLEPRRVAARAAARRLATllgeaPGETVGYRVRGES------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 277 kkfgpKSSKKFDILVTTPNRLIYLLKQEPpgiDLTSVEWLVVDE-------SDKLFE---DGKTGFRDQLASIflactsp 346
Cdd:cd17990 87 -----RVGRRTRVEVVTEGVLLRRLQRDP---ELSGVGAVILDEfhersldADLALAlllEVQQLLRDDLRLL------- 151
|
170 180 190
....*....|....*....|....*....|
gi 16758984 347 kvrrAMfSATFayDVEQWCKLnLDNIVSVS 376
Cdd:cd17990 152 ----AM-SATL--DGDGLAAL-LPEAPVVE 173
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
188-321 |
1.38e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 39.58 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 188 VPTPIQMQAI----PVMLHGRE-LLASAPTGSGKTL-AFSIPILMQLKQPTNKgfrALVISPTRELASQIHRELIKISEG 261
Cdd:pfam04851 3 ELRPYQIEAIenllESIKNGQKrGLIVMATGSGKTLtAAKLIARLFKKGPIKK---VLFLVPRKDLLEQALEEFKKFLPN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16758984 262 TGFRIhmihkaAIAAKKFGPKSSKKFDILVTTPNRL--IYLLKQEPPGIDLTSVewLVVDES 321
Cdd:pfam04851 80 YVEIG------EIISGDKKDESVDDNKIVVTTIQSLykALELASLELLPDFFDV--IIIDEA 133
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
202-320 |
1.52e-03 |
|
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: 39.86 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 202 HGRELLASAPtGSGKTLAfSIPILMQLKQPTNKGFRALVISPtrelASQIH---RELIKISEGtgFRIHMIHKA-AIAAK 277
Cdd:cd17919 19 GPGGILADEM-GLGKTLQ-AIAFLAYLLKEGKERGPVLVVCP----LSVLEnweREFEKWTPD--LRVVVYHGSqRERAQ 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 16758984 278 KFGPKSSKKFDILVTTPNRLIYLLKQeppgidLTSVEW--LVVDE 320
Cdd:cd17919 91 IRAKEKLDKFDVVLTTYETLRRDKAS------LRKFRWdlVVVDE 129
|
|
| PRK09751 |
PRK09751 |
putative ATP-dependent helicase Lhr; Provisional |
444-505 |
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 16758984 444 HAERTQQQRDNTVHSFRAGKIWVLICTALLARGIDFKGVNLVINYDFPTSSVEYIHRIGRTG 505
Cdd:PRK09751 308 HGSVSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
|
|
| DEAHc_XPD-like |
cd17915 |
DEAH-box helicase domain of XPD family DEAD-like helicases; The xeroderma pigmentosum group D ... |
210-324 |
2.01e-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: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 210 APTGSGKTLaFSIPILMQLkQPTNKGFRALVISPTRELASQIHRELIKISEGTGFRihmihkaaiaakkFGPKSSKKFDI 289
Cdd:cd17915 8 SPTGSGKTL-SLLCSALSY-QREFHKTKVLYCSRTHSQIEQIIRELRKLLEKRKIR-------------ALALSSRDADI 72
|
90 100 110
....*....|....*....|....*....|....*
gi 16758984 290 LVTTPNRLIYLLKQEPPGIDLtSVEWLVVDESDKL 324
Cdd:cd17915 73 VVLPYPYLLDARIREFIGIDL-REQVVIIDEAHNL 106
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
210-247 |
3.21e-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: 38.35 E-value: 3.21e-03
10 20 30
....*....|....*....|....*....|....*...
gi 16758984 210 APTGSGKTLAFSIPILMQLkqptNKGFRALVISPTREL 247
Cdd:cd01127 6 GTTGSGKTTSIVIPLLDQA----ARGGSVIITDPKGEL 39
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
207-320 |
3.26e-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: 39.17 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758984 207 LASAPTGSGKTLafsIPILM------QLKQPTNKGFRALVISPTRELASQIHRElikISEGTGFRIHMIHKA---AIAAK 277
Cdd:cd18034 20 IVVLPTGSGKTL---IAVMLikemgeLNRKEKNPKKRAVFLVPTVPLVAQQAEA---IRSHTDLKVGEYSGEmgvDKWTK 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 16758984 278 KFGPKSSKKFDILVTTPNRLIYLLKQeppG-IDLTSVEWLVVDE 320
Cdd:cd18034 94 ERWKEELEKYDVLVMTAQILLDALRH---GfLSLSDINLLIFDE 134
|
|
| |
