|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
62-480 |
2.55e-160 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 461.54 E-value: 2.55e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 62 TWKDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRY-FALVLTPTRE 140
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRApQALILAPTRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 141 LAFQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENmKGFNLKAIKYLVMDEADRILNMD 220
Cdd:COG0513 83 LALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRMLDMG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 221 FEVELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKVEVSNKYQTVEQLQQSYLFIPVKYKDVYLVHILNELAG 300
Cdd:COG0513 162 FIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDEDP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 301 NSFMIFCSTCNNTVKTALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDVVVNFDIPTH 380
Cdd:COG0513 242 ERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLPED 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 381 SKDYIHRVGRTARAGRSGKAITLVSQYDIELYQRIEHLLGKQLTLYKCEEDEVmALQERVAEAQRTAKLELKDLEDTRGG 460
Cdd:COG0513 322 PEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEP-VEEKRLERLKPKIKEKLKGKKAGRGG 400
|
410 420
....*....|....*....|
gi 24585582 461 HKRGGDTHDDSENFTGARKR 480
Cdd:COG0513 401 RPGPKGERKARRGKRRRRKR 420
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
62-264 |
2.93e-153 |
|
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: 434.82 E-value: 2.93e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 62 TWKDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYFALVLTPTREL 141
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 142 AFQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKGFNLKAIKYLVMDEADRILNMDF 221
Cdd:cd17954 81 AQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLNMDF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24585582 222 EVELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKVE 264
Cdd:cd17954 161 EPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
64-264 |
7.32e-98 |
|
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: 293.75 E-value: 7.32e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 64 KDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYFALVLTPTRELAF 143
Cdd:cd17955 2 EDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 144 QIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKG--FNLKAIKYLVMDEADRILNMDF 221
Cdd:cd17955 82 QIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttKVLSRVKFLVLDEADRLLTGSF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24585582 222 EVELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKVE 264
Cdd:cd17955 162 EDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
66-423 |
4.00e-94 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 293.63 E-value: 4.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 66 LGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALleNPQRYF--ALVLTPTRELAF 143
Cdd:PRK11776 9 LPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL--DVKRFRvqALVLCPTRELAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 144 QIGEQFEALGSGI-GIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLEnmKG-FNLKAIKYLVMDEADRILNMDF 221
Cdd:PRK11776 87 QVAKEIRRLARFIpNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLR--KGtLDLDALNTLVLDEADRMLDMGF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 222 EVELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKVEVSNKYQ--TVEQLqqsylFIPVKYKDVY--LVHILNE 297
Cdd:PRK11776 165 QDAIDAIIRQAPARRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDlpAIEQR-----FYEVSPDERLpaLQRLLLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 298 LAGNSFMIFCSTCNNTVKTALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDVVVNFDI 377
Cdd:PRK11776 240 HQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYEL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 24585582 378 PTHSKDYIHRVGRTARAGRSGKAITLVSQYDIELYQRIEHLLGKQL 423
Cdd:PRK11776 320 ARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLGRKL 365
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
72-264 |
1.77e-91 |
|
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: 277.40 E-value: 1.77e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 72 LCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYF----ALVLTPTRELAFQIGE 147
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGrgpqALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 148 QFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENmKGFNLKAIKYLVMDEADRILNMDFEVELDK 227
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIER-GKLDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 24585582 228 ILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKVE 264
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
62-423 |
2.86e-86 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 272.20 E-value: 2.86e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 62 TWKDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYFA----LVLTP 137
Cdd:PRK11192 2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGppriLILTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 138 TRELAFQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKgFNLKAIKYLVMDEADRIL 217
Cdd:PRK11192 82 TRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEEN-FDCRAVETLILDEADRML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 218 NMDFEVELDKILKVLPRERRTFLFSATMT-KKVKKLQRASLKDPVKVEVSNKYQTVEQLQQSY-LFIPVKYKDVYLVHIL 295
Cdd:PRK11192 161 DMGFAQDIETIAAETRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKKIHQWYyRADDLEHKTALLCHLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 296 NELAGNSFMIFCSTCNNTVKTALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDVVVNF 375
Cdd:PRK11192 241 KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVINF 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 24585582 376 DIPTHSKDYIHRVGRTARAGRSGKAITLVSQYDIELYQRIEHLLGKQL 423
Cdd:PRK11192 321 DMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPL 368
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
58-459 |
3.36e-84 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 272.88 E-value: 3.36e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 58 EQKLTWKDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHAL---LENPQryfALV 134
Cdd:PRK11634 3 EFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLdpeLKAPQ---ILV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 135 LTPTRELAFQIGEQFEALGSGI-GIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLEnmKG-FNLKAIKYLVMDE 212
Cdd:PRK11634 80 LAPTRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLK--RGtLDLSKLSGLVLDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 213 ADRILNMDFEVELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKVEVSNKYQTVEQLQQSYLFIPVKYKDVYLV 292
Cdd:PRK11634 158 ADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 293 HILNELAGNSFMIFCSTCNNTVKTALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDVV 372
Cdd:PRK11634 238 RFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 373 VNFDIPTHSKDYIHRVGRTARAGRSGKAITLVSQYDIELYQRIEHLLgkQLTLYKCEEDEVMALQERVAE---AQRTAKL 449
Cdd:PRK11634 318 VNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTM--KLTIPEVELPNAELLGKRRLEkfaAKVQQQL 395
|
410
....*....|
gi 24585582 450 ELKDLEDTRG 459
Cdd:PRK11634 396 ESSDLDQYRA 405
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
61-423 |
4.71e-82 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 262.05 E-value: 4.71e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 61 LTWKDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQR------YFALV 134
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 135 LTPTRELAFQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDhLENMKGFNLKAIKYLVMDEAD 214
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 215 RILNMDFEVELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKVEVSNKYQTVEQLQQSYLFIPVKYKDVYLVHI 294
Cdd:PRK10590 160 RMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 295 LNELAGNSFMIFCSTCNNTVKTALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDVVVN 374
Cdd:PRK10590 240 IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 24585582 375 FDIPTHSKDYIHRVGRTARAGRSGKAITLVSQYDIELYQRIEHLLGKQL 423
Cdd:PRK10590 320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEI 368
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
82-402 |
2.06e-79 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 257.78 E-value: 2.06e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 82 KAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALP-ILHALLENPQRY----FALVLTPTRELAFQIGEQFEALGSGI 156
Cdd:PTZ00110 151 TEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPaIVHINAQPLLRYgdgpIVLVLAPTRELAEQIREQCNKFGASS 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 157 GIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENmKGFNLKAIKYLVMDEADRILNMDFEVELDKILKVLPRER 236
Cdd:PTZ00110 231 KIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLES-NVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIRPDR 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 237 RTFLFSATMTKKVKKLQRASLKD-PVKVEV-SNKYQTVEQLQQSYLFIPVKYKDVYLVHILNEL--AGNSFMIFCSTCNN 312
Cdd:PTZ00110 310 QTLMWSATWPKEVQSLARDLCKEePVHVNVgSLDLTACHNIKQEVFVVEEHEKRGKLKMLLQRImrDGDKILIFVETKKG 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 313 TVKTALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTA 392
Cdd:PTZ00110 390 ADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTG 469
|
330
....*....|
gi 24585582 393 RAGRSGKAIT 402
Cdd:PTZ00110 470 RAGAKGASYT 479
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
72-263 |
1.31e-76 |
|
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: 239.08 E-value: 1.31e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 72 LCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYF---ALVLTPTRELAFQIGEQ 148
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAatrVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 149 FEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKGFNLKAIKYLVMDEADRILNMDFEVELDKI 228
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....*
gi 24585582 229 LKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKV 263
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVRV 195
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
52-429 |
1.39e-72 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 237.89 E-value: 1.39e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 52 EDDAAEEQ--KLTWKDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENP-- 127
Cdd:PRK01297 76 EDFVVEPQegKTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPpp 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 128 -QRYF----ALVLTPTRELAFQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQL-AKKPHIIIATPGRLVDHLENmKGFN 201
Cdd:PRK01297 156 kERYMgeprALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQR-GEVH 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 202 LKAIKYLVMDEADRILNMDFEVELDKILKVLPR--ERRTFLFSATMTKKVKKLQRASLKDPVKVEVSNKYQTVEQLQQSY 279
Cdd:PRK01297 235 LDMVEVMVLDEADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 280 LFIPVKYKDVYLVHILNELAGNSFMIFCSTCNNTVKTALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRSILISTDV 359
Cdd:PRK01297 315 YAVAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDV 394
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 360 ASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITLVSQYDIELYQRIEHLLGKQLtlyKCE 429
Cdd:PRK01297 395 AGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKI---SCE 461
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
61-483 |
1.54e-69 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 232.53 E-value: 1.54e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 61 LTWKDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALL-------ENPQRYFAL 133
Cdd:PRK04537 9 LTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLsrpaladRKPEDPRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 134 VLTPTRELAFQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKGFNLKAIKYLVMDEA 213
Cdd:PRK04537 89 ILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVLDEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 214 DRILNMDFEVELDKILKVLPRE--RRTFLFSATMTKKVKKLQRASLKDPVKVEVSNKYQTVEQLQQSYLFIPVKYKDVYL 291
Cdd:PRK04537 169 DRMFDLGFIKDIRFLLRRMPERgtRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 292 VHILNELAGNSFMIFCSTCNNTVKTALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDV 371
Cdd:PRK04537 249 LGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKY 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 372 VVNFDIPTHSKDYIHRVGRTARAGRSGKAITL------VSQYDIELY--QRI--EHLLGKQLT-LYKCEEDEVM------ 434
Cdd:PRK04537 329 VYNYDLPFDAEDYVHRIGRTARLGEEGDAISFaceryaMSLPDIEAYieQKIpvEPVTAELLTpLPRPPRVPVEgeeadd 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24585582 435 ------------ALQERVAEAQRTAKLELKDLEDTRGGHKRGGDTHDDSENFTGARKRMKP 483
Cdd:PRK04537 409 eagdsvgtifreAREQRAAEEQRRGGGRSGPGGGSRSGSVGGGGRRDGAGADGKPRPRRKP 469
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
85-252 |
8.09e-64 |
|
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: 204.78 E-value: 8.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 85 SKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYFALVLTPTRELAFQIGEQFEALGSGIGIKCCVVV 164
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 165 GGMDMVAQgLQLAKKPHIIIATPGRLVDHLENMKgfNLKAIKYLVMDEADRILNMDFEVELDKILKVLPRERRTFLFSAT 244
Cdd:pfam00270 81 GGDSRKEQ-LEKLKGPDILVGTPGRLLDLLQERK--LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157
|
....*...
gi 24585582 245 MTKKVKKL 252
Cdd:pfam00270 158 LPRNLEDL 165
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
58-417 |
9.07e-64 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 213.29 E-value: 9.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 58 EQKLTwkDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQ---RYF--- 131
Cdd:PRK04837 7 EQKFS--DFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPApedRKVnqp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 132 -ALVLTPTRELAFQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENmKGFNLKAIKYLVM 210
Cdd:PRK04837 85 rALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQ-NHINLGAIQVVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 211 DEADRILNMDFEVELDKILKVLP--RERRTFLFSATMTKKVKKLQRASLKDPVKVEVSNKYQTVEQLQQSyLFIPVK-YK 287
Cdd:PRK04837 164 DEADRMFDLGFIKDIRWLFRRMPpaNQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEE-LFYPSNeEK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 288 DVYLVHILNELAGNSFMIFCSTCNNTVKTALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRSILISTDVASRGLDIP 367
Cdd:PRK04837 243 MRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARGLHIP 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 24585582 368 HVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITLV-SQY-----DIELYqrIEH 417
Cdd:PRK04837 323 AVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLAcEEYalnlpAIETY--IGH 376
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
72-263 |
1.89e-63 |
|
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: 206.02 E-value: 1.89e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 72 LCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRY--------FALVLTPTRELAF 143
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeetkddgpYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 144 QIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENmKGFNLKAIKYLVMDEADRILNMDFEV 223
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLER-RLLVLNQCTYVVLDEADRMIDMGFEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 224 ELDKILKVLP--------------------RERRTFLFSATMTKKVKKLQRASLKDPVKV 263
Cdd:cd17945 160 QVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPVVV 219
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
62-259 |
8.44e-62 |
|
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: 201.56 E-value: 8.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 62 TWKDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRY----------F 131
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSvgrgrrkaypS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 132 ALVLTPTRELAFQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLEnmKGF-NLKAIKYLVM 210
Cdd:cd17967 81 ALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIE--RGRiSLSSIKFLVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24585582 211 DEADRILNMDFEVELDKILK----VLPRERRTFLFSATMTKKVKKLQRASLKD 259
Cdd:cd17967 159 DEADRMLDMGFEPQIRKIVEhpdmPPKGERQTLMFSATFPREIQRLAADFLKN 211
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
62-263 |
9.50e-62 |
|
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: 200.99 E-value: 9.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 62 TWKDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRY--FALVLTPTR 139
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTVgaRALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 140 ELAFQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMkGFNLKAIKYLVMDEADRILNM 219
Cdd:cd17959 82 ELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEM-NLKLSSVEYVVFDEADRLFEM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24585582 220 DFEVELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKV 263
Cdd:cd17959 161 GFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
38-423 |
1.27e-61 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 206.99 E-value: 1.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 38 DSEAALSGEDDKGSEDDAAEeqklTWKDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFAL 117
Cdd:PTZ00424 9 QSEQVASTGTIESNYDEIVD----SFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 118 PILHALLENPQRYFALVLTPTRELAFQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENm 197
Cdd:PTZ00424 85 AALQLIDYDLNACQALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDK- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 198 KGFNLKAIKYLVMDEADRILNMDFEVELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKVEVSNKYQTVEQLQQ 277
Cdd:PTZ00424 164 RHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 278 SYLFI-PVKYKDVYLVHILNELAGNSFMIFCSTCNNTVKTALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRSILIS 356
Cdd:PTZ00424 244 FYVAVeKEEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLIT 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24585582 357 TDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITLVSQYDIELYQRIEHLLGKQL 423
Cdd:PTZ00424 324 TDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERHYNTQI 390
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
74-272 |
1.61e-59 |
|
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: 196.31 E-value: 1.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 74 QACDELKWKAPSKIQREAIPVAL-QGKDVIGLAETGSGKTGAFALPILHALLE--------NPQRY-FALVLTPTRELAF 143
Cdd:cd17946 3 RALADLGFSEPTPIQALALPAAIrDGKDVIGAAETGSGKTLAFGIPILERLLSqkssngvgGKQKPlRALILTPTRELAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 144 QIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKGF--NLKAIKYLVMDEADRIL-NMD 220
Cdd:cd17946 83 QVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHlaNLKSLRFLVLDEADRMLeKGH 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 221 FEvELDKILKVLPRE-------RRTFLFSATMTKKV-KKLQRASLKDPVKVEVSNKYQTV 272
Cdd:cd17946 163 FA-ELEKILELLNKDragkkrkRQTFVFSATLTLDHqLPLKLNSKKKKKKKEKKQKLELL 221
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
68-261 |
1.58e-58 |
|
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: 192.41 E-value: 1.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 68 LNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLE------NPQRYFALVLTPTREL 141
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKakaesgEEQGTRALILVPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 142 AFQIGEQFEALGSGIG--IKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKGFNLKAIKYLVMDEADRILNM 219
Cdd:cd17961 81 AQQVSKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLSY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24585582 220 DFEVELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPV 261
Cdd:cd17961 161 GYEEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
67-265 |
1.33e-56 |
|
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: 187.11 E-value: 1.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 67 GLNEAlcqacdelKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYF----ALVLTPTRELA 142
Cdd:cd17941 4 GLKEA--------GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTPEdglgALIISPTRELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 143 FQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKpHIIIATPGRLVDHLENMKGFNLKAIKYLVMDEADRILNMDFE 222
Cdd:cd17941 76 MQIFEVLRKVGKYHSFSAGLIIGGKDVKEEKERINRM-NILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24585582 223 VELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKVEV 265
Cdd:cd17941 155 ETLDAIVENLPKSRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
275-404 |
8.77e-56 |
|
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: 182.71 E-value: 8.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 275 LQQSYLFIPVKYKDVYL-VHILNELAGNSFMIFCSTCNNTVKTALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRSI 353
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 24585582 354 LISTDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITLV 404
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
78-263 |
3.05e-55 |
|
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: 183.72 E-value: 3.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 78 ELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALP-ILHALLENPQRY----FALVLTPTRELAFQIGEQFEAL 152
Cdd:cd17966 7 RQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPaIVHINAQPPLERgdgpIVLVLAPTRELAQQIQQEANKF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 153 GSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKGfNLKAIKYLVMDEADRILNMDFEVELDKILKVL 232
Cdd:cd17966 87 GGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKT-NLRRVTYLVLDEADRMLDMGFEPQIRKIVDQI 165
|
170 180 190
....*....|....*....|....*....|.
gi 24585582 233 PRERRTFLFSATMTKKVKKLQRASLKDPVKV 263
Cdd:cd17966 166 RPDRQTLMWSATWPKEVRRLAEDFLKDYIQV 196
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
72-265 |
6.57e-55 |
|
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: 182.79 E-value: 6.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 72 LCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQR--YFALVLTPTRELAFQIGEQF 149
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKkgLRALILAPTRELASQIYREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 150 EALGSGIGIKCCVVVGGM-DMVAQGLQLAKKPHIIIATPGRLVDHLENMKgFNLKAIKYLVMDEADRILNMDFEVELDKI 228
Cdd:cd17957 81 LKLSKGTGLRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQGP-IDLSSVEYLVLDEADKLFEPGFREQTDEI 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 24585582 229 LKVL--PRERRTFlFSATMTKKVKKLQRASLKDPVKVEV 265
Cdd:cd17957 160 LAACtnPNLQRSL-FSATIPSEVEELARSVMKDPIRIIV 197
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
54-419 |
1.10e-54 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 191.54 E-value: 1.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 54 DAAEEQKLTWKDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPIL-------HALLEN 126
Cdd:PLN00206 114 EAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIIsrcctirSGHPSE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 127 PQRYFALVLTPTRELAFQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKgFNLKAIK 206
Cdd:PLN00206 194 QRNPLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTPGRLIDLLSKHD-IELDNVS 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 207 YLVMDEADRILNMDFEVELDKILKVLPRERrTFLFSATMTKKVKKLQRASLKDPVKVEVSNKYQTVEQLQQSYLFIPVKY 286
Cdd:PLN00206 273 VLVLDEVDCMLERGFRDQVMQIFQALSQPQ-VLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQ 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 287 KDVYLVHILneLAGNSFM----IFCstcNNTVKTALMLRAL----GLAAIPLHGQMSQNKRLAALNKFKAKNRSILISTD 358
Cdd:PLN00206 352 KKQKLFDIL--KSKQHFKppavVFV---SSRLGADLLANAItvvtGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATG 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24585582 359 VASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITLVSQYDIELYQRIEHLL 419
Cdd:PLN00206 427 VLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALL 487
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
79-261 |
2.95e-54 |
|
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: 181.63 E-value: 2.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 79 LKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRY------FALVLTPTRELAFQIGEQFEAL 152
Cdd:cd17949 9 MGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVdrsdgtLALVLVPTRELALQIYEVLEKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 153 GSG-IGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKGFNLKAIKYLVMDEADRILNMDFEVELDKILKV 231
Cdd:cd17949 89 LKPfHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILEL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24585582 232 L-------------PRERRTFLFSATMTKKVKKLQRASLKDPV 261
Cdd:cd17949 169 LddkrskaggekskPSRRQTVLVSATLTDGVKRLAGLSLKDPV 211
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
61-263 |
4.30e-54 |
|
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: 181.42 E-value: 4.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 61 LTWKDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENP-----QRYFALVL 135
Cdd:cd17953 12 QKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRpvkpgEGPIGLIM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 136 TPTRELAFQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHL--ENMKGFNLKAIKYLVMDEA 213
Cdd:cd17953 92 APTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVTNLRRVTYVVLDEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24585582 214 DRILNMDFEVELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKV 263
Cdd:cd17953 172 DRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
68-258 |
1.90e-53 |
|
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: 179.32 E-value: 1.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 68 LNEALCQACDELKWKAPSKIQREAIPVALQ-GKDVIGLAETGSGKTGAFALPILHALLENPQRY-----FALVLTPTREL 141
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGrrsgvSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 142 AFQIGEQFEALGSGI-GIKCCVVVGGMDMVAQGLQLAK-KPHIIIATPGRLVDHLEN-MKGFNLKAIKYLVMDEADRILN 218
Cdd:cd17964 81 ALQIAAEAKKLLQGLrKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLENpGVAKAFTDLDYLVLDEADRLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24585582 219 MDFEVELDKILKVLP----RERRTFLFSATMTKKVKKLQRASLK 258
Cdd:cd17964 161 MGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTLK 204
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
78-266 |
3.96e-53 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 178.07 E-value: 3.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 78 ELKWKAPSKIQREAIPVALQG-KDVIGLAETGSGKTGAFALPILHALLENPQRYfALVLTPTRELAFQIGEQFEALGSGI 156
Cdd:smart00487 3 KFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGGR-VLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 157 GIKCCVVVGGMDMVAQGLQLAK-KPHIIIATPGRLVDHLENmKGFNLKAIKYLVMDEADRILNMDFEVELDKILKVLPRE 235
Cdd:smart00487 82 GLKVVGLYGGDSKREQLRKLESgKTDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKN 160
|
170 180 190
....*....|....*....|....*....|.
gi 24585582 236 RRTFLFSATMTKKVKKLQRASLKDPVKVEVS 266
Cdd:smart00487 161 VQLLLLSATPPEEIENLLELFLNDPVFIDVG 191
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
75-260 |
1.16e-52 |
|
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: 176.78 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 75 ACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALP---ILHALLENPQRYFA-LVLTPTRELAFQIGEQFE 150
Cdd:cd17942 4 AIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPaieLLYKLKFKPRNGTGvIIISPTRELALQIYGVAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 151 ALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKGFNLKAIKYLVMDEADRILNMDFEVELDKILK 230
Cdd:cd17942 84 ELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQIIK 163
|
170 180 190
....*....|....*....|....*....|
gi 24585582 231 VLPRERRTFLFSATMTKKVKKLQRASLKDP 260
Cdd:cd17942 164 LLPKRRQTMLFSATQTRKVEDLARISLKKK 193
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
74-263 |
1.43e-52 |
|
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: 176.61 E-value: 1.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 74 QACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALL-----ENPQRYFALVLTPTRELAFQIGEQ 148
Cdd:cd17960 3 DVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLkrkanLKKGQVGALIISPTRELATQIYEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 149 FEALGSGIG--IKCCVVVGGMDMVAQGLQL-AKKPHIIIATPGRLVDHLENMKG-FNLKAIKYLVMDEADRILNMDFEVE 224
Cdd:cd17960 83 LQSFLEHHLpkLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRKADkVKVKSLEVLVLDEADRLLDLGFEAD 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 24585582 225 LDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKV 263
Cdd:cd17960 163 LNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVRV 201
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
72-263 |
2.89e-51 |
|
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: 172.98 E-value: 2.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 72 LCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRY-----FALVLTPTRELAFQIG 146
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEkgegpIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 147 EQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLEnMKGFNLKAIKYLVMDEADRILNMDFEVELD 226
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVK-KKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 24585582 227 KILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKV 263
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIRV 196
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
78-263 |
5.99e-51 |
|
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350709 [Multi-domain] Cd Length: 206 Bit Score: 172.52 E-value: 5.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 78 ELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRY--------FALVLTPTRELA---FQIG 146
Cdd:cd17951 7 KKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLpfikgegpYGLIVCPSRELArqtHEVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 147 EQFEALGSGIG---IKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLeNMKGFNLKAIKYLVMDEADRILNMDFEV 223
Cdd:cd17951 87 EYYCKALQEGGypqLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDML-NKKKINLDICRYLCLDEADRMIDMGFEE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24585582 224 ELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKV 263
Cdd:cd17951 166 DIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
63-263 |
3.47e-49 |
|
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: 167.86 E-value: 3.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 63 WKDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALleNPQRYF--ALVLTPTRE 140
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKI--DPKKDViqALILVPTRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 141 LAFQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLEnmKGF-NLKAIKYLVMDEADRILNM 219
Cdd:cd17940 79 LALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAK--KGVaDLSHCKTLVLDEADKLLSQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24585582 220 DFEVELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKV 263
Cdd:cd17940 157 DFQPIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYEI 200
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
62-259 |
4.10e-46 |
|
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: 161.36 E-value: 4.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 62 TWKDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLEN--------PQRYF-- 131
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgeslpsESGYYgr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 132 ------ALVLTPTRELAFQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKgFNLKAI 205
Cdd:cd18051 102 rkqyplALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGK-IGLDYC 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24585582 206 KYLVMDEADRILNMDFEVELDKILK--VLPR--ERRTFLFSATMTKKVKKLQRASLKD 259
Cdd:cd18051 181 KYLVLDEADRMLDMGFEPQIRRIVEqdTMPPtgERQTLMFSATFPKEIQMLARDFLDN 238
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
65-263 |
1.49e-45 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 158.26 E-value: 1.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 65 DLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYFALVLTPTRELAFQ 144
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 145 IGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLeNMKGFNLKAIKYLVMDEADRILNMDFEVE 224
Cdd:cd17939 81 IQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDML-QRRSLRTDKIKMFVLDEADEMLSRGFKDQ 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 24585582 225 LDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKV 263
Cdd:cd17939 160 IYDIFQFLPPETQVVLFSATMPHEVLEVTKKFMRDPVRI 198
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
61-284 |
5.94e-45 |
|
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA homolog) is an ATP-dependent RNA helicase required during spermatogenesis and is essential for the germline integrity. DEAD-box helicases are a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350810 [Multi-domain] Cd Length: 264 Bit Score: 158.59 E-value: 5.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 61 LTWKDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLEN---------PQRYF 131
Cdd:cd18052 43 LTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgltassfseVQEPQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 132 ALVLTPTRELAFQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKgFNLKAIKYLVMD 211
Cdd:cd18052 123 ALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGK-ISLSKLKYLILD 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24585582 212 EADRILNMDFEVELDKILKVL--PR--ERRTFLFSATMTKKVKKLQRaslkdpvkvevsnkyqtvEQLQQSYLFIPV 284
Cdd:cd18052 202 EADRMLDMGFGPEIRKLVSEPgmPSkeDRQTLMFSATFPEEIQRLAA------------------EFLKEDYLFLTV 260
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
81-263 |
2.00e-44 |
|
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: 155.01 E-value: 2.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 81 WKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYFALVLTPTRELAFQIGEQFEALGSGI-GIK 159
Cdd:cd17962 10 YEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMKGLpPMK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 160 CCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLeNMKGFNLKAIKYLVMDEADRILNMDFEVELDKILKVLPRERRTF 239
Cdd:cd17962 90 TALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDIL-KQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHDHQTI 168
|
170 180
....*....|....*....|....
gi 24585582 240 LFSATMTKKVKKLQRASLKDPVKV 263
Cdd:cd17962 169 LVSATIPRGIEQLAGQLLQNPVRI 192
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
84-263 |
4.80e-44 |
|
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis antigen 13 or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 is also called cancer/testis antigen 26 or DEAD-Box Protein CAGE. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350716 [Multi-domain] Cd Length: 197 Bit Score: 154.16 E-value: 4.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 84 PSKIQREAIPVALQGKDVIGLAETGSGKTGAFALP-ILHALLENPQRY-----FALVLTPTRELAFQIGEQFEALgSGIG 157
Cdd:cd17958 13 PSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgFIHLDLQPIPREqrngpGVLVLTPTRELALQIEAECSKY-SYKG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 158 IKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDhLENMKGFNLKAIKYLVMDEADRILNMDFEVELDKILKVLPRERR 237
Cdd:cd17958 92 LKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGFEPQIRKILLDIRPDRQ 170
|
170 180
....*....|....*....|....*.
gi 24585582 238 TFLFSATMTKKVKKLQRASLKDPVKV 263
Cdd:cd17958 171 TIMTSATWPDGVRRLAQSYLKDPMIV 196
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
65-252 |
2.35e-42 |
|
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: 149.78 E-value: 2.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 65 DLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILhallenpQRYFALVLTPTRELAFQ 144
Cdd:cd17938 3 ELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-------QIVVALILEPSRELAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 145 IGEQFEALGSGI---GIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKgFNLKAIKYLVMDEADRILNMDF 221
Cdd:cd17938 76 TYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGK-LDLSSVRFFVLDEADRLLSQGN 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 24585582 222 EVELDKILKVLP----RERR--TFLFSATM-TKKVKKL 252
Cdd:cd17938 155 LETINRIYNRIPkitsDGKRlqVIVCSATLhSFEVKKL 192
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
72-260 |
1.82e-41 |
|
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: 148.16 E-value: 1.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 72 LCQACDELKWKAPSKIQREAIPVALQG---------KDVIGLAETGSGKTGAFALPILHALLENP-QRYFALVLTPTREL 141
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVvPRLRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 142 AFQIGEQFEALGSGIGIKCCVVVGGMD--------MVAQGLQLAKKPHIIIATPGRLVDHLENMKGFNLKAIKYLVMDEA 213
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVVSLSGQKSfkkeqkllLVDTSGRYLSRVDILVATPGRLVDHLNSTPGFTLKHLRFLVIDEA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24585582 214 DRILNMDFEVELDKILKVLPRERRT--------------------FLFSATMTKKVKKLQRASLKDP 260
Cdd:cd17956 161 DRLLNQSFQDWLETVMKALGRPTAPdlgsfgdanllersvrplqkLLFSATLTRDPEKLSSLKLHRP 227
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
64-265 |
3.28e-41 |
|
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: 146.72 E-value: 3.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 64 KDLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYFALVLTPTRELAF 143
Cdd:cd17950 5 RDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 144 QIGEQFEALGSGI-GIKCCVVVGGMDMVAQGLQLAKK-PHIIIATPGRLVDHLENmKGFNLKAIKYLVMDEADRIL-NMD 220
Cdd:cd17950 85 QISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKNKcPHIVVGTPGRILALVRE-KKLKLSHVKHFVLDECDKMLeQLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24585582 221 FEVELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKVEV 265
Cdd:cd17950 164 MRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPLEIFV 208
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
83-264 |
7.19e-40 |
|
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: 142.79 E-value: 7.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 83 APSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYFALVLTPTRELAFQIGEQFEALGSGI-GIKCC 161
Cdd:cd17943 12 RPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKKIGKKLeGLKCE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 162 VVVGGMDmVAQGLQLAKKPHIIIATPGRLVdHLENMKGFNLKAIKYLVMDEADRILNMDFEVELDKILKVLPRERRTFLF 241
Cdd:cd17943 92 VFIGGTP-VKEDKKKLKGCHIAVGTPGRIK-QLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSSLPKNKQVIAF 169
|
170 180
....*....|....*....|...
gi 24585582 242 SATMTKKVKKLQRASLKDPVKVE 264
Cdd:cd17943 170 SATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
81-265 |
1.20e-39 |
|
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: 143.61 E-value: 1.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 81 WKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALP-ILH----ALLENPQRYFALVLTPTRELAFQIGEQFEALGSG 155
Cdd:cd18049 44 FTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPaIVHinhqPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 156 IGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKGfNLKAIKYLVMDEADRILNMDFEVELDKILKVLPRE 235
Cdd:cd18049 124 CRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPD 202
|
170 180 190
....*....|....*....|....*....|
gi 24585582 236 RRTFLFSATMTKKVKKLQRASLKDPVKVEV 265
Cdd:cd18049 203 RQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
65-263 |
1.62e-38 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350804 [Multi-domain] Cd Length: 201 Bit Score: 139.50 E-value: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 65 DLGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYFALVLTPTRELAFQ 144
Cdd:cd18046 3 DMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKATQALVLAPTRELAQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 145 IGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLeNMKGFNLKAIKYLVMDEADRILNMDFEVE 224
Cdd:cd18046 83 IQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMI-NRRYLRTDYIKMFVLDEADEMLSRGFKDQ 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 24585582 225 LDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKV 263
Cdd:cd18046 162 IYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIRI 200
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
80-265 |
3.14e-38 |
|
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: 140.92 E-value: 3.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 80 KWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALP-ILH----ALLENPQRYFALVLTPTRELAFQIGEQFEALGS 154
Cdd:cd18050 81 NFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPaIVHinhqPYLERGDGPICLVLAPTRELAQQVQQVADDYGK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 155 GIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKGfNLKAIKYLVMDEADRILNMDFEVELDKILKVLPR 234
Cdd:cd18050 161 SSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRP 239
|
170 180 190
....*....|....*....|....*....|.
gi 24585582 235 ERRTFLFSATMTKKVKKLQRASLKDPVKVEV 265
Cdd:cd18050 240 DRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
68-263 |
1.24e-37 |
|
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: 136.94 E-value: 1.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 68 LNEALCQACDELKWKAPSKIQREAIPVALQG--KDVIGLAETGSGKTGAFALPILHALLEN---PQryfALVLTPTRELA 142
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRVDPTlksPQ---ALCLAPTRELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 143 FQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAkkpHIIIATPGRLVDHLENMKgFNLKAIKYLVMDEADRILNMD-F 221
Cdd:cd17963 78 RQIGEVVEKMGKFTGVKVALAVPGNDVPRGKKITA---QIVIGTPGTVLDWLKKRQ-LDLKKIKILVLDEADVMLDTQgH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24585582 222 EVELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKV 263
Cdd:cd17963 154 GDQSIRIKRMLPRNCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
287-395 |
7.41e-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: 123.47 E-value: 7.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 287 KDVYLVHILNELAGNSFMIFCSTCNnTVKTALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRSILISTDVASRGLDI 366
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKK-TLEAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 24585582 367 PHVDVVVNFDIPTHSKDYIHRVGRTARAG 395
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
66-263 |
6.30e-30 |
|
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: 116.03 E-value: 6.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 66 LGLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYFALVLTPTRELAFQI 145
Cdd:cd18045 4 MGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELAVQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 146 GEQFEALGSGIGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENmKGFNLKAIKYLVMDEADRILNMDFEVEL 225
Cdd:cd18045 84 QKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADEMLNKGFKEQI 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 24585582 226 DKILKVLPRERRTFLFSATMTKKVKKLQRASLKDPVKV 263
Cdd:cd18045 163 YDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIRI 200
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
84-252 |
2.21e-29 |
|
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: 115.54 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 84 PSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALL---ENPQRYF----ALVLTPTRELAFQIGEQFEALGSGI 156
Cdd:cd17948 13 PTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLrykLLAEGPFnaprGLVITPSRELAEQIGSVAQSLTEGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 157 GIKCCVVVGGmdmvaQGLQLAKKPH-----IIIATPGRLVDhLENMKGFNLKAIKYLVMDEADRILNMDFEVELDKILK- 230
Cdd:cd17948 93 GLKVKVITGG-----RTKRQIRNPHfeevdILVATPGALSK-LLTSRIYSLEQLRHLVLDEADTLLDDSFNEKLSHFLRr 166
|
170 180 190
....*....|....*....|....*....|....
gi 24585582 231 ------------VLPRERRTFLFSATMTKKVKKL 252
Cdd:cd17948 167 fplasrrsentdGLDPGTQLVLVSATMPSGVGEV 200
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
317-395 |
1.60e-27 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 105.37 E-value: 1.60e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24585582 317 ALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAG 395
Cdd:smart00490 4 AELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
87-258 |
1.60e-24 |
|
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: 101.08 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 87 IQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYF------ALVLTPTRELAFQIGEQFEALGSGIGIKC 160
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKrgrapkVLVLAPTRELANQVTKDFKDITRKLSVAC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 161 cvVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKgFNLKAIKYLVMDEADRILNMDFEVELDKILKVLPRER---- 236
Cdd:cd17944 96 --FYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGR-LDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSYKKDsedn 172
|
170 180
....*....|....*....|...
gi 24585582 237 -RTFLFSATMTKKVKKLQRASLK 258
Cdd:cd17944 173 pQTLLFSATCPDWVYNVAKKYMK 195
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
98-244 |
5.06e-23 |
|
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: 94.78 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 98 GKDVIGLAETGSGKTGAFALPILHALLEnpQRYFALVLTPTRELAFQIGEQFEALGSgIGIKCCVVVGGMDMVAQGLQLA 177
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERLRELFG-PGIRVAVLVGGSSAEEREKNKL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24585582 178 KKPHIIIATPGRLVDHLENMKGFNLKAIKYLVMDEADRIL-NMDFEVELD-KILKVLPRERRTFLFSAT 244
Cdd:cd00046 78 GDADIIIATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLiDSRGALILDlAVRKAGLKNAQVILLSAT 146
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
62-260 |
5.10e-23 |
|
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: 97.40 E-value: 5.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 62 TWKDLGLNEALCQACDELKWKAPSKIQREAIPVALQG--KDVIGLAETGSGKTGAFALPIL---HALLENPQryfALVLT 136
Cdd:cd18048 19 SFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLsrvDALKLYPQ---CLCLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 137 PTRELAFQIGEQFEALGS-GIGIKCCVVVGGmDMVAQGLQLAKKphIIIATPGRLVDHLENMKGFNLKAIKYLVMDEADR 215
Cdd:cd18048 96 PTFELALQTGKVVEEMGKfCVGIQVIYAIRG-NRPGKGTDIEAQ--IVIGTPGTVLDWCFKLRLIDVTNISVFVLDEADV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24585582 216 ILNMD-FEVELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDP 260
Cdd:cd18048 173 MINVQgHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
62-260 |
3.61e-20 |
|
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: 88.62 E-value: 3.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 62 TWKDLGLNEALCQACDELKWKAPSKIQREAIPVALQG--KDVIGLAETGSGKTGAFALPILHALLENPQRYFALVLTPTR 139
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 140 ELAFQIGEQFEALGSGI-GIKCCVVVGGMDMvAQGLQLakKPHIIIATPGRLVDHLENMKGFNLKAIKYLVMDEAD-RIL 217
Cdd:cd18047 82 ELALQTGKVIEQMGKFYpELKLAYAVRGNKL-ERGQKI--SEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADvMIA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24585582 218 NMDFEVELDKILKVLPRERRTFLFSATMTKKVKKLQRASLKDP 260
Cdd:cd18047 159 TQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
88-482 |
2.76e-19 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 90.85 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 88 QREAI-----PVALQGKDVIGLAETGSGKTGAFALpILHALLENPQryfALVLTPTRELAFQIGEQFEALGSGIGIKccv 162
Cdd:COG1061 85 QQEALeallaALERGGGRGLVVAPTGTGKTVLALA-LAAELLRGKR---VLVLVPRRELLEQWAEELRRFLGDPLAG--- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 163 vvggmdmvaqGLQLAKKPHIIIATPGRLV--DHLENMKgfnlKAIKYLVMDEADRILNMDFEveldKILKVLPRERRtFL 240
Cdd:COG1061 158 ----------GGKKDSDAPITVATYQSLArrAHLDELG----DRFGLVIIDEAHHAGAPSYR----RILEAFPAAYR-LG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 241 FSAT------------------MTKKVKKLQRAS-LKDPVKVEVS-------NKYQTVEQLQQSYLFIPVKYKDVYLVHI 294
Cdd:COG1061 219 LTATpfrsdgreillflfdgivYEYSLKEAIEDGyLAPPEYYGIRvdltderAEYDALSERLREALAADAERKDKILREL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 295 LNELAGNSF-MIFCSTcNNTVKT-ALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDVV 372
Cdd:COG1061 299 LREHPDDRKtLVFCSS-VDHAEAlAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRLDVA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 373 VNFDiPTHSK-DYIHRVGRTARAGRSGKAITLvsqYDI---------ELYQRIEHLLGKQLTL---YKCEEDEVMALQER 439
Cdd:COG1061 378 ILLR-PTGSPrEFIQRLGRGLRPAPGKEDALV---YDFvgndvpvleELAKDLRDLAGYRVEFldeEESEELALLIAVKP 453
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 24585582 440 VAEAQRTAKLELKDLEDTRGGHKRGGDTHDDSENFTGARKRMK 482
Cdd:COG1061 454 ALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELL 496
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
84-254 |
2.09e-16 |
|
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: 78.96 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 84 PSKIQREAIPVALQ----------GKDVIGL------AETGSGKTGAFALPILHALLENPQRYF---------------- 131
Cdd:cd17965 31 PSPIQTLAIKKLLKtlmrkvtkqtSNEEPKLevfllaAETGSGKTLAYLAPLLDYLKRQEQEPFeeaeeeyesakdtgrp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 132 -ALVLTPTRELAFQIGEQFEALGSGIGIKCCVVVGGMDMVAQGLQLA--KKPHIIIATPGRLVDHLE-NMKgfNLKAIKY 207
Cdd:cd17965 111 rSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQRLQLAfkGRIDILVTTPGKLASLAKsRPK--ILSRVTH 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24585582 208 LVMDEADRILNMDFEVELDKILKVLPRERRTFLFSATMTKKVKKLQR 254
Cdd:cd17965 189 LVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLR 235
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
67-213 |
1.11e-14 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 76.80 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 67 GLNEALCQACDELKWKAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPqRYFALVLTPTRELAFqig 146
Cdd:COG1205 40 WLPPELRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP-GATALYLYPTKALAR--- 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24585582 147 EQFEAL-----GSGIGIKCCVVVGGMDMvAQGLQLAKKPHIIIATP-----GrLVDHLENMKGFnLKAIKYLVMDEA 213
Cdd:COG1205 116 DQLRRLrelaeALGLGVRVATYDGDTPP-EERRWIREHPDIVLTNPdmlhyG-LLPHHTRWARF-FRNLRYVVIDEA 189
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
320-404 |
5.31e-13 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 71.30 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 320 LRALGLAAIPLHGQ--------MSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDVVVNFD-IPTHSKdYIHRVGR 390
Cdd:COG1111 373 LSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpVPSEIR-SIQRKGR 451
|
90
....*....|....
gi 24585582 391 TARaGRSGKAITLV 404
Cdd:COG1111 452 TGR-KREGRVVVLI 464
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
86-244 |
6.63e-12 |
|
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: 64.21 E-value: 6.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 86 KIQREAI-PVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRyfALVLTPTRELAFQIGEQFEALGSGIGIKCCVVV 164
Cdd:cd17921 4 PIQREALrALYLSGDSVLVSAPTSSGKTLIAELAILRALATSGGK--AVYIAPTRALVNQKEADLRERFGPLGKNVGLLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 165 GgmDMVAQGLQLAKkPHIIIATPGRLVDHLENMKGFNLKAIKYLVMDEA----DRILNMDFEVELDKILKVLPRERRTFL 240
Cdd:cd17921 82 G--DPSVNKLLLAE-ADILVATPEKLDLLLRNGGERLIQDVRLVVVDEAhligDGERGVVLELLLSRLLRINKNARFVGL 158
|
....
gi 24585582 241 fSAT 244
Cdd:cd17921 159 -SAT 161
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
320-406 |
1.65e-11 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 66.82 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 320 LRALGLAAIPLHGQ--------MSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDVVVNFD-IPTHSKdYIHRVGR 390
Cdd:PRK13766 385 LEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIR-SIQRKGR 463
|
90
....*....|....*.
gi 24585582 391 TARaGRSGKAITLVSQ 406
Cdd:PRK13766 464 TGR-QEEGRVVVLIAK 478
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
88-323 |
1.95e-11 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 66.07 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 88 QREAIPVAL-QGKDVIGLAETGSGKTGAFALPILHALLENPQryfALVLTPTRELAFQIGEQFEALGSGIGIKCCVVVGG 166
Cdd:COG1204 27 QAEALEAGLlEGKNLVVSAPTASGKTLIAELAILKALLNGGK---ALYIVPLRALASEKYREFKRDFEELGIKVGVSTGD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 167 MDmvaQGLQLAKKPHIIIATPGRLvDHLENMKGFNLKAIKYLVMDEA------DR--ILnmdfEVELDKILKVLPRERRT 238
Cdd:COG1204 104 YD---SDDEWLGRYDILVATPEKL-DSLLRNGPSWLRDVDLVVVDEAhliddeSRgpTL----EVLLARLRRLNPEAQIV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 239 FLfSATMtKKVKKLqrASLKDPVKVEVSnkYQTVEQLQqsYLFIP--VKYKDVYLV----------HILNElaGNSFMIF 306
Cdd:COG1204 176 AL-SATI-GNAEEI--AEWLDAELVKSD--WRPVPLNE--GVLYDgvLRFDDGSRRskdptlalalDLLEE--GGQVLVF 245
|
250
....*....|....*..
gi 24585582 307 CSTCNNTVKTALMLRAL 323
Cdd:COG1204 246 VSSRRDAESLAKKLADE 262
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
88-213 |
1.04e-10 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 60.68 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 88 QREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYfALVLTPTRELAfqiGEQFEAL-----GSGIGIKCCV 162
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSR-ALYLYPTKALA---QDQLRSLrelleQLGLGIRVAT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24585582 163 VVGGMDMVAQGLQLAKKPHIIIATP-----------GRLVDHLENMkgfnlkaiKYLVMDEA 213
Cdd:cd17923 81 YDGDTPREERRAIIRNPPRILLTNPdmlhyallphhDRWARFLRNL--------RYVVLDEA 134
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
333-394 |
2.55e-10 |
|
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: 58.37 E-value: 2.55e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24585582 333 QMSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRtARA 394
Cdd:cd18802 73 LMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
352-404 |
4.45e-10 |
|
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: 55.79 E-value: 4.45e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 24585582 352 SILISTDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAG-RSGKAITLV 404
Cdd:cd18785 24 EILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
334-403 |
1.29e-09 |
|
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: 56.60 E-value: 1.29e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 334 MSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARaGRSGKAITL 403
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVVVL 142
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
88-414 |
2.67e-09 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 59.73 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 88 QREAIPVALQGKDVIGLAETGSGKTGAFALPilhALLENPqryFALVLTPTRELAFQIGEQFEAlgSGIGIKCCVVVGGM 167
Cdd:PRK11057 30 QQEIIDAVLSGRDCLVVMPTGGGKSLCYQIP---ALVLDG---LTLVVSPLISLMKDQVDQLLA--NGVAAACLNSTQTR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 168 DM---VAQGLQLAKKPHIIIAtPGRLV--DHLENMKGFNLKAIkylVMDEADRI--LNMDFEVELdkilKVLPRERRTF- 239
Cdd:PRK11057 102 EQqleVMAGCRTGQIKLLYIA-PERLMmdNFLEHLAHWNPALL---AVDEAHCIsqWGHDFRPEY----AALGQLRQRFp 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 240 -----LFSATMTKKVKK--LQRASLKDPVkVEVSN------KYQTVEqlqqsylfipvKYKDV-YLVHILNELAGNSFMI 305
Cdd:PRK11057 174 tlpfmALTATADDTTRQdiVRLLGLNDPL-IQISSfdrpniRYTLVE-----------KFKPLdQLMRYVQEQRGKSGII 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 306 FCSTCNNTVKTALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDVVVNFDIPTHSKDYI 385
Cdd:PRK11057 242 YCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYY 321
|
330 340
....*....|....*....|....*....
gi 24585582 386 HRVGRTARAGRSGKAITLVSQYDIELYQR 414
Cdd:PRK11057 322 QETGRAGRDGLPAEAMLFYDPADMAWLRR 350
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
88-244 |
1.14e-08 |
|
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: 54.65 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 88 QREAI-PVALQGKDVIGLAETGSGKTGAFALPILHALLENPQryfALVLTPTRELAFQIGEQFEALgSGIGIKCCVVVGG 166
Cdd:cd18028 6 QAEAVrAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGGK---ALYLVPLRALASEKYEEFKKL-EEIGLKVGISTGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 167 MDMVAQGLqlaKKPHIIIATPGRLvDHLENMKGFNLKAIKYLVMDEADRILNMD----FEVELDKILKVLPrERRTFLFS 242
Cdd:cd18028 82 YDEDDEWL---GDYDIIVATYEKF-DSLLRHSPSWLRDVGVVVVDEIHLISDEErgptLESIVARLRRLNP-NTQIIGLS 156
|
..
gi 24585582 243 AT 244
Cdd:cd18028 157 AT 158
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
98-212 |
1.59e-08 |
|
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: 54.13 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 98 GKDVIGLAETGSGKTGAFALPILHALLENPQRYFALV-LTPTRELAFQIGEQFEALGSGIGIKCCVVVGGMDmVAQGL-- 174
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEKGVQVLyISPLKALINDQERRLEEPLDEIDLEIPVAVRHGD-TSQSEka 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 24585582 175 -QLAKKPHIIIATPgrlvDHLENM---KGFN--LKAIKYLVMDE 212
Cdd:cd17922 80 kQLKNPPGILITTP----ESLELLlvnKKLRelFAGLRYVVVDE 119
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
88-263 |
1.60e-08 |
|
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: 54.85 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 88 QREAIPVALQGKDVIGLAETGSGKTGAFALPilhALLENPqryFALVLTPTRELafqIGEQFEALgSGIGIKCCVVVGGM 167
Cdd:cd17920 17 QLEAINAVLAGRDVLVVMPTGGGKSLCYQLP---ALLLDG---VTLVVSPLISL---MQDQVDRL-QQLGIRAAALNSTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 168 DM--VAQGLQLAKKP--HIIIATPGRLV-----DHLENMKGFNLkaIKYLVMDEADRILN--MDFE---VELDKILKVLP 233
Cdd:cd17920 87 SPeeKREVLLRIKNGqyKLLYVTPERLLspdflELLQRLPERKR--LALIVVDEAHCVSQwgHDFRpdyLRLGRLRRALP 164
|
170 180 190
....*....|....*....|....*....|..
gi 24585582 234 RErRTFLFSATMTKKVKK--LQRASLKDPVKV 263
Cdd:cd17920 165 GV-PILALTATATPEVREdiLKRLGLRNPVIF 195
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
86-187 |
4.89e-08 |
|
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: 53.51 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 86 KIQREAIPVALQG-KDVIGLAETGSGKTGAFALPILHALLENPQ----RYFALVLTPTRELAFQIGEQFEALGSGIGIKC 160
Cdd:cd18023 4 RIQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERNPlpwgNRKVVYIAPIKALCSEKYDDWKEKFGPLGLSC 83
|
90 100
....*....|....*....|....*..
gi 24585582 161 CVVVGgmDMVAQGLQLAKKPHIIIATP 187
Cdd:cd18023 84 AELTG--DTEMDDTFEIQDADIILTTP 108
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
291-378 |
1.30e-07 |
|
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: 50.55 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 291 LVHILNELAGNS--FMIFCstcnNTVKT----ALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRS--ILISTDVASR 362
Cdd:cd18793 16 LLELLEELREPGekVLIFS----QFTDTldilEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGV 91
|
90
....*....|....*.
gi 24585582 363 GLDIPHVDVVVNFDIP 378
Cdd:cd18793 92 GLNLTAANRVILYDPW 107
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
84-213 |
1.49e-07 |
|
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 51.88 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 84 PSKIQREAIPVALQgKDVIGLAETGSGKTGAFALPILH-----ALLENPQRyFALVLTPTRELAFQigeQFEALGSGIGI 158
Cdd:cd18034 3 PRSYQLELFEAALK-RNTIVVLPTGSGKTLIAVMLIKEmgelnRKEKNPKK-RAVFLVPTVPLVAQ---QAEAIRSHTDL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 24585582 159 KCCVVVGGM--DMVAQG--LQLAKKPHIIIATPGRLVDHLENMKgFNLKAIKYLVMDEA 213
Cdd:cd18034 78 KVGEYSGEMgvDKWTKErwKEELEKYDVLVMTAQILLDALRHGF-LSLSDINLLIFDEC 135
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
287-414 |
1.86e-07 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 53.61 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 287 KDVYLVHILNELAGNSFMIFCSTCNNTVKTALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRSILISTdVA-SRGLD 365
Cdd:COG0514 217 KLAQLLDFLKEHPGGSGIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGID 295
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 24585582 366 IPHVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITLVSQYDIELYQR 414
Cdd:COG0514 296 KPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRF 344
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
80-129 |
2.36e-07 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 53.57 E-value: 2.36e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 24585582 80 KWKAPSKIQREAIPVALQGKDVIGLAETGSGKT-GAFaLPILHALLENPQR 129
Cdd:COG1201 21 RFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPRP 70
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
88-258 |
5.01e-07 |
|
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) 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 in RecQ2 cause Bloom syndrome.
Pssm-ID: 350774 [Multi-domain] Cd Length: 208 Bit Score: 50.60 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 88 QREAIPVALQGKDVIGLAETGSGKTGAFALPILhaLLENpqryFALVLTPTRELafqIGEQFEALGSgIGIKCCVVVGGM 167
Cdd:cd18016 22 QLEAINAALLGEDCFVLMPTGGGKSLCYQLPAC--VSPG----VTVVISPLRSL---IVDQVQKLTS-LDIPATYLTGDK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 168 DMVAQG---LQLAKKPHII---------IATPGRLVDHLENMKGFNLkaIKYLVMDEADRI--LNMDFEVELDKiLKVLp 233
Cdd:cd18016 92 TDAEATkiyLQLSKKDPIIkllyvtpekISASNRLISTLENLYERKL--LARFVIDEAHCVsqWGHDFRPDYKR-LNML- 167
|
170 180
....*....|....*....|....*....
gi 24585582 234 RER----RTFLFSATMTKKVKKLQRASLK 258
Cdd:cd18016 168 RQKfpsvPMMALTATATPRVQKDILNQLK 196
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
86-366 |
7.67e-07 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 51.62 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 86 KIQREAIPVALQGKDVIGL-AETGSGKTGAFALPIL-HALLENPQR-YFALvltPTRELAFQIGEQFEALG--------S 154
Cdd:COG1203 134 EALELALEAAEEEPGLFILtAPTGGGKTEAALLFALrLAAKHGGRRiIYAL---PFTSIINQTYDRLRDLFgedvllhhS 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 155 GIGIKCCVVVGGMDMVAQGLQLAKK----PhIIIATPGRLVDHLE-NMKGFNLK----AIKYLVMDEADrilnmDFEVE- 224
Cdd:COG1203 211 LADLDLLEEEEEYESEARWLKLLKElwdaP-VVVTTIDQLFESLFsNRKGQERRlhnlANSVIILDEVQ-----AYPPYm 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 225 ---LDKILKVLPRERRTFLF-SATMTKkvkkLQRASLKDPVKVeVSNKYQTVEQLQQSYLFIPVKYK------DVYLVHI 294
Cdd:COG1203 285 lalLLRLLEWLKNLGGSVILmTATLPP----LLREELLEAYEL-IPDEPEELPEYFRAFVRKRVELKegplsdEELAELI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 295 LNELA-GNSFMIFCstcnNTVKTALML-RAL--GLAAIP---LHGQMSQNKRLAALNK----FKAKNRSILISTDVASRG 363
Cdd:COG1203 360 LEALHkGKSVLVIV----NTVKDAQELyEALkeKLPDEEvylLHSRFCPADRSEIEKEikerLERGKPCILVSTQVVEAG 435
|
...
gi 24585582 364 LDI 366
Cdd:COG1203 436 VDI 438
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
88-419 |
1.08e-06 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 51.44 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 88 QREAIPVALQGKDVIGLAETGSGKTGAFALPilhALLENPqryFALVLTPTRELafqIGEQFEALGSGiGIKCCVVVGGM 167
Cdd:PLN03137 465 QREIINATMSGYDVFVLMPTGGGKSLTYQLP---ALICPG---ITLVISPLVSL---IQDQIMNLLQA-NIPAASLSAGM 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 168 DMVAQGLQLAK------KPHIIIATPGR------LVDHLENMKGFNLKAikYLVMDEADRI--LNMDFEVELDK--ILKV 231
Cdd:PLN03137 535 EWAEQLEILQElsseysKYKLLYVTPEKvaksdsLLRHLENLNSRGLLA--RFVIDEAHCVsqWGHDFRPDYQGlgILKQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 232 LPRERRTFLFSATMTKKVKK--LQRASLKDPVKVEvsnkyQTVEQLQQSYLFIPVKYKdvYLVHILNELAGNSF----MI 305
Cdd:PLN03137 613 KFPNIPVLALTATATASVKEdvVQALGLVNCVVFR-----QSFNRPNLWYSVVPKTKK--CLEDIDKFIKENHFdecgII 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 306 FCSTCNNTVKTALMLRALGLAAIPLHGQMSQNKRlAALNKFKAKNRSILISTDVA-SRGLDIPHVDVVVNFDIPTHSKDY 384
Cdd:PLN03137 686 YCLSRMDCEKVAERLQEFGHKAAFYHGSMDPAQR-AFVQKQWSKDEINIICATVAfGMGINKPDVRFVIHHSLPKSIEGY 764
|
330 340 350
....*....|....*....|....*....|....*
gi 24585582 385 IHRVGrtaRAGRSGKAITLVSQYDIELYQRIEHLL 419
Cdd:PLN03137 765 HQECG---RAGRDGQRSSCVLYYSYSDYIRVKHMI 796
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
304-393 |
1.58e-06 |
|
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: 46.78 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 304 MIFCSTCNNTVKTALMLRALGLAAIPLHGQMSQNKRL---AALNKFKAKNRSILISTDVASRGLDIPHVDVVVnFDIPTH 380
Cdd:cd18799 10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdeaLILLFFGELKPPILVTVDLLTTGVDIPEVDNVV-FLRPTE 88
|
90
....*....|....
gi 24585582 381 SKD-YIHRVGRTAR 393
Cdd:cd18799 89 SRTlFLQMLGRGLR 102
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
291-378 |
6.53e-06 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 48.68 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 291 LVHILNEL--AGNSFMIFCSTcnntVKTALM----LRALGLAAIPLHGQMSQNKRLAALNKFKAKNRS--ILISTDVASR 362
Cdd:COG0553 538 LLELLEELlaEGEKVLVFSQF----TDTLDLleerLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLISLKAGGE 613
|
90
....*....|....*.
gi 24585582 363 GLDIPHVDVVVNFDIP 378
Cdd:COG0553 614 GLNLTAADHVIHYDLW 629
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
88-212 |
1.02e-04 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 45.26 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 88 QREAIPVALQGKDVIGLAETGSGKTGAFALPILHAL--------LENpqRYFALVLTPTRELA-----------FQIGEQ 148
Cdd:PRK13767 37 QRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELfrlgregeLED--KVYCLYVSPLRALNndihrnleeplTEIREI 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24585582 149 FEALGSGI-GIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKgFN--LKAIKYLVMDE 212
Cdd:PRK13767 115 AKERGEELpEIRVAIRTGDTSSYEKQKMLKKPPHILITTPESLAILLNSPK-FRekLRTVKWVIVDE 180
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
330-395 |
1.97e-04 |
|
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: 41.87 E-value: 1.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 330 LHGQMSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDVVVNFDIPTHSKDYIH----RVGRTARAG 395
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHqlrgRVGRGKHQS 135
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
335-401 |
3.19e-04 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 42.23 E-value: 3.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24585582 335 SQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVD--VVVNFDIPTHSKDY---------IHRV-GRTARAGRSGKAI 401
Cdd:cd18804 129 KKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTlvGILNADSGLNSPDFraserafqlLTQVsGRAGRGDKPGKVI 207
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
305-399 |
3.88e-04 |
|
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: 40.65 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 305 IFCSTCNNTVKTALMLRALGLAAIPLHGQMSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDVVVNFDIPTHSKDY 384
Cdd:cd18794 35 IYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESY 114
|
90
....*....|....*
gi 24585582 385 IHRVGrtaRAGRSGK 399
Cdd:cd18794 115 YQESG---RAGRDGL 126
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
84-215 |
5.84e-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: 41.26 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 84 PSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYFA--LVLTPTRELAFQIGEQFEALGSGIGIKCC 161
Cdd:cd17927 3 PRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGkvVFLANKVPLVEQQKEVFRKHFERPGYKVT 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 24585582 162 VVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKGFNLKAIKYLVMDEADR 215
Cdd:cd17927 83 GLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
88-213 |
5.94e-04 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350773 [Multi-domain] Cd Length: 209 Bit Score: 41.20 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 88 QREAIPVALQGKDVIGLAETGSGKTGAFALPilhALLENPqryFALVLTPTRELafqIGEQFEALGSgIGIKCCVVVGGM 167
Cdd:cd18015 23 QLETINATMAGRDVFLVMPTGGGKSLCYQLP---ALCSDG---FTLVVSPLISL---MEDQLMALKK-LGISATMLNASS 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 24585582 168 D-----MVAQGLQLAKKP-HIIIATP------GRLVDHLEnmKGFNLKAIKYLVMDEA 213
Cdd:cd18015 93 SkehvkWVHAALTDKNSElKLLYVTPekiaksKRFMSKLE--KAYNAGRLARIAIDEV 148
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
330-390 |
7.41e-04 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 40.41 E-value: 7.41e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24585582 330 LHGQMSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDVVVNFDIPTHSKDYIH----RVGR 390
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDAERFGLSQLHqlrgRVGR 131
|
|
| rad25 |
TIGR00603 |
DNA repair helicase rad25; All proteins in this family for which functions are known are ... |
317-481 |
1.15e-03 |
|
DNA repair helicase rad25; All proteins in this family for which functions are known are DNA-DNA helicases used for the initiation of nucleotide excision repair and transacription as part of the TFIIH complex.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273168 [Multi-domain] Cd Length: 732 Bit Score: 41.71 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 317 ALMLRALGLAAIPLHGQMSQNKRLAALNKFK--AKNRSILISTdVASRGLDIPHVDVVVNfdIPTHS---KDYIHRVGRT 391
Cdd:TIGR00603 508 ALKEYAIKLGKPFIYGPTSQQERMQILQNFQhnPKVNTIFLSK-VGDTSIDLPEANVLIQ--ISSHYgsrRQEAQRLGRI 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 392 ARAGRSGKAI-------TLVSQYDIELY-----QR-----------IEHLLG----KQLTlYKCEEDEVMALQERVAEAQ 444
Cdd:TIGR00603 585 LRAKKGSDAEeynaffySLVSKDTQEMYystkrQRflvdqgysfkvITHLPGmdneSNLA-YSSKEEQLELLQKVLLAGD 663
|
170 180 190
....*....|....*....|....*....|....*..
gi 24585582 445 RTAKLElkDLEDTRGGHKRGGDTHDDSENFTGARKRM 481
Cdd:TIGR00603 664 LDAELE--VLEGEFGSRALGASRSMSSASGKAVRRGG 698
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
81-187 |
1.26e-03 |
|
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: 39.93 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 81 WKAPSKIQREAIPVALQGKD-VIGLAETGSGKTGAFALPILHALLENP-QRyfALVLTPTRELAFQIGEQFEA-LGSGIG 157
Cdd:cd18021 1 FKFFNPIQTQVFNSLYNTDDnVFVGAPTGSGKTVCAELALLRHWRQNPkGR--AVYIAPMQELVDARYKDWRAkFGPLLG 78
|
90 100 110
....*....|....*....|....*....|
gi 24585582 158 IKCCVVVGGMdmvAQGLQLAKKPHIIIATP 187
Cdd:cd18021 79 KKVVKLTGET---STDLKLLAKSDVILATP 105
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
337-458 |
1.29e-03 |
|
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350185 [Multi-domain] Cd Length: 174 Bit Score: 39.60 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 337 NKRLAALNKFKAKNRSILI----STDVASRGLDIPH-VDVVVNFDIPTHSkdYIHRVGRTAR--AGRSGKAITLVSQYDI 409
Cdd:cd18798 59 SSTEKNLEKFEEGEIDVLIgvasYYGVLVRGIDLPErIKYAIFYGVPVTT--YIQASGRTSRlyAGGLTKGLSVVLVDDP 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 24585582 410 ELYqrieHLLGKQLTLYkceedevmaLQERVAEAQRTAKLE--LKDLEDTR 458
Cdd:cd18798 137 ELF----EALKKRLKLI---------LDEFIFKELEEVDLEelLSEIDESR 174
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
208-396 |
1.58e-03 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 40.88 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 208 LVMDEADRIL---NMDFEveldKILKVLPRERRTF-LFSATMTKKVKKLQRASlkDPVKVEVSNKYQTVEQlqqsYLFIP 283
Cdd:cd09639 127 LIFDEVHFYDeytLALIL----AVLEVLKDNDVPIlLMSATLPKFLKEYAEKI--GYVEENEPLDLKPNER----APFIK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 284 VKYKDVYLVHILNEL-----AGNSFMIFCstcnNTVKTA----LMLRALGLAA--IPLHGQMSQNKRLAA----LNKFKA 348
Cdd:cd09639 197 IESDKVGEISSLERLlefikKGGSVAIIV----NTVDRAqefyQQLKEKGPEEeiMLIHSRFTEKDRAKKeaelLLEFKK 272
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24585582 349 KNRSILISTDVASRGLDIpHVDVVVNFDIPTHSkdYIHRVGRTARAGR 396
Cdd:cd09639 273 SEKFVIVATQVIEASLDI-SVDVMITELAPIDS--LIQRLGRLHRYGE 317
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
88-244 |
1.61e-03 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 38.83 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 88 QREAIPVALQGKD----VIGLAeTGSGKTgAFALPILHALLENPqryfALVLTPTRELAFQIGEQFEALGSGIGIKccvV 163
Cdd:cd17926 5 QEEALEAWLAHKNnrrgILVLP-TGSGKT-LTALALIAYLKELR----TLIVVPTDALLDQWKERFEDFLGDSSIG---L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 164 VGGMDMVAQGLQLakkphIIIATPGRLVDHLEN-MKGFNLKAikYLVMDEADRILNMDFEveldKILKVLPRERRtFLFS 242
Cdd:cd17926 76 IGGGKKKDFDDAN-----VVVATYQSLSNLAEEeKDLFDQFG--LLIVDEAHHLPAKTFS----EILKELNAKYR-LGLT 143
|
..
gi 24585582 243 AT 244
Cdd:cd17926 144 AT 145
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
330-404 |
2.14e-03 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 38.86 E-value: 2.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24585582 330 LHGQMSQNKRLAALNKFKAKNRSILISTDVASRGLDIPHVDVVVNFDIPTHSKDYIHRV-GRTARAGRSGKAITLV 404
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKERAYAYFLY 132
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
87-245 |
3.21e-03 |
|
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 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: 350730 [Multi-domain] Cd Length: 234 Bit Score: 39.43 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 87 IQREAIPVA----------LQGKDVIGLAETGSGKTGAFALPILHALLENPQ-RYFALVLT-PTRELAFQIGEQ--FEAl 152
Cdd:cd17972 54 QERELLPVKkfreeileaiSNNPVVIIRGATGCGKTTQVPQYILDDFIQNDRaAECNIVVTqPRRISAVSVAERvaFER- 132
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 153 GSGIGIKCCVVVggmdmvaQGLQLAKKPH--IIIATPGRLVDHLENmkgfNLKAIKYLVMDEA-DRILNMDFE-VELDKI 228
Cdd:cd17972 133 GEEVGKSCGYSV-------RFESVLPRPHasILFCTVGVLLRKLEA----GIRGISHVIVDEIhERDINTDFLlVVLRDV 201
|
170
....*....|....*..
gi 24585582 229 LKVLPrERRTFLFSATM 245
Cdd:cd17972 202 VQAYP-DLRVILMSATI 217
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|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
82-212 |
3.85e-03 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350831 [Multi-domain] Cd Length: 202 Bit Score: 38.65 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 82 KAPSKIQREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENPQRYFALVLTptreLAFQIG--EQ----FEALGSG 155
Cdd:cd18073 1 FKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVF----FATKVPvyEQqksvFSKYFER 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 24585582 156 IGIKCCVVVGGMDMVAQGLQLAKKPHIIIATPGRLVDHLENMKGFNLKAIKYLVMDE 212
Cdd:cd18073 77 HGYRVTGISGATAENVPVEQIIENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDE 133
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
287-401 |
4.34e-03 |
|
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: 37.63 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 287 KDVYLVHILNELAGNSFMIFCSTCNNTVKTALMLRALGLA-----AIPLH-GQMSQNKRLAALNKFKAKNRSILISTDVA 360
Cdd:cd18796 25 ADAYAEVIFLLERHKSTLVFTNTRSQAERLAQRLRELCPDrvppdFIALHhGSLSRELREEVEAALKRGDLKVVVATSSL 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 24585582 361 SRGLDIPHVDVVVNFDIPTHSKDYIHRVGrtaRAGRSGKAI 401
Cdd:cd18796 105 ELGIDIGDVDLVIQIGSPKSVARLLQRLG---RSGHRPGAA 142
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|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
88-196 |
5.15e-03 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 38.23 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585582 88 QREAIPVALQGKDVIGLAETGSGKTGAFALPILHALLENP---QRYFALVLTPTRELAFQIGEQFEALGSGiGIKCCVVV 164
Cdd:cd18036 7 QLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRsagEKGRVVVLVNKVPLVEQQLEKFFKYFRK-GYKVTGLS 85
|
90 100 110
....*....|....*....|....*....|..
gi 24585582 165 GGMDMVAQGLQLAKKPHIIIATPGRLVDHLEN 196
Cdd:cd18036 86 GDSSHKVSFGQIVKASDVIICTPQILINNLLS 117
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