|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
23-453 |
5.02e-158 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 453.45 E-value: 5.02e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 23 TKTFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQR-LFALVLTPT 101
Cdd:COG0513 1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRaPQALILAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 102 RELAFQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENtKGFNLRALKYLVMDEADRILN 181
Cdd:COG0513 81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRMLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 182 MDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYLFIPSKFKDTYLVYILNEL 261
Cdd:COG0513 160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 262 AGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIP 341
Cdd:COG0513 240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 342 THSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIEHLIGKKLPVFPTQDEEVmmlterVNEAQRFARMElrehgEKK 421
Cdd:COG0513 320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIEEEELPGFEP------VEEKRLERLKP-----KIK 388
|
410 420 430
....*....|....*....|....*....|..
gi 26345792 422 KRKREDAGDDDDKEGAIGVRNKvAGGKMKKRK 453
Cdd:COG0513 389 EKLKGKKAGRGGRPGPKGERKA-RRGKRRRRK 419
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
25-227 |
7.99e-155 |
|
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: 437.13 E-value: 7.99e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 25 TFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTREL 104
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 105 AFQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDF 184
Cdd:cd17954 81 AQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLNMDF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 26345792 185 ETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCA 227
Cdd:cd17954 161 EPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
24-446 |
2.92e-95 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 293.77 E-value: 2.92e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 24 KTFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFA----LVLT 99
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGppriLILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 100 PTRELAFQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKgFNLRALKYLVMDEADRI 179
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEEN-FDCRAVETLILDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 180 LNMDFETEVDKILKVIpRDRK-TFLFSATMT-KKVQKLQRAALKNPVKCAVSSKYQTVEKLQQ-YYLFIPSKFKDTYLVY 256
Cdd:PRK11192 160 LDMGFAQDIETIAAET-RWRKqTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKKIHQwYYRADDLEHKTALLCH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 257 ILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVV 336
Cdd:PRK11192 239 LLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 337 NFDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIEHLIGKKLP------VFPTQDEEVMMLTERVNEAQRFA 410
Cdd:PRK11192 319 NFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLKarvideLRPKTKAPSEKKTGKPSKKVLAK 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 26345792 411 RMELREHGEKKKRKREDAGDDDdkegAIGVRNKVAG 446
Cdd:PRK11192 399 RAEKKEKEKEKPKVKKRHRDTK----NIGKRRKPSG 430
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
26-227 |
3.18e-93 |
|
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: 280.26 E-value: 3.18e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 26 FKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELA 105
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 106 FQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKG--FNLRALKYLVMDEADRILNMD 183
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttKVLSRVKFLVLDEADRLLTGS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 26345792 184 FETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCA 227
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
40-390 |
8.01e-92 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 285.93 E-value: 8.01e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 40 DQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELAFQISEQFEALGSSI 119
Cdd:PRK11776 20 NELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQVAKEIRRLARFI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 120 -GVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLEntKG-FNLRALKYLVMDEADRILNMDFETEVDKILKVIPR 197
Cdd:PRK11776 100 pNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLR--KGtLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 198 DRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYLFIPSKfKDTYLVYILNELAGNSFMIFCSTCNNTQ 277
Cdd:PRK11776 178 RRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPAIEQRFYEVSPDE-RLPALQRLLLHHQPESCVVFCNTKKECQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 278 RTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARA 357
Cdd:PRK11776 257 EVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRA 336
|
330 340 350
....*....|....*....|....*....|...
gi 26345792 358 GRSGKAITFVTQYDVELFQRIEHLIGKKLPVFP 390
Cdd:PRK11776 337 GSKGLALSLVAPEEMQRANAIEDYLGRKLNWEP 369
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
25-368 |
1.73e-90 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 285.13 E-value: 1.73e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 25 TFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPIL-----NALLETPQRLFALVLT 99
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIvhinaQPLLRYGDGPIVLVLA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 100 PTRELAFQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKGfNLRALKYLVMDEADRI 179
Cdd:PTZ00110 211 PTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVT-NLRRVTYLVLDEADRM 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 180 LNMDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKN-PVKCAVSS-KYQTVEKLQQYYLFIPSKFKDTYLVYI 257
Cdd:PTZ00110 290 LDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSlDLTACHNIKQEVFVVEEHEKRGKLKML 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 258 LNEL--AGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVV 335
Cdd:PTZ00110 370 LQRImrDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYV 449
|
330 340 350
....*....|....*....|....*....|...
gi 26345792 336 VNFDIPTHSKDYIHRVGRTARAGRSGKAITFVT 368
Cdd:PTZ00110 450 INFDFPNQIEDYVHRIGRTGRAGAKGASYTFLT 482
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
35-225 |
3.68e-90 |
|
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: 272.01 E-value: 3.68e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 35 LCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLF----ALVLTPTRELAFQISE 110
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGrgpqALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 111 QFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKgFNLRALKYLVMDEADRILNMDFETEVDK 190
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGK-LDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*
gi 26345792 191 ILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVK 225
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVR 194
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
20-387 |
1.18e-86 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 277.50 E-value: 1.18e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 20 EEETkTFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNAL---LETPQrlfAL 96
Cdd:PRK11634 3 EFET-TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLdpeLKAPQ---IL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 97 VLTPTRELAFQISEQFEALGSSI-GVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKgFNLRALKYLVMDE 175
Cdd:PRK11634 79 VLAPTRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGT-LDLSKLSGLVLDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 176 ADRILNMDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYLFIPSKFKDTYLV 255
Cdd:PRK11634 158 ADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 256 YILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVV 335
Cdd:PRK11634 238 RFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 26345792 336 VNFDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIEHLIGKKLP 387
Cdd:PRK11634 318 VNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIP 369
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
25-455 |
1.58e-77 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 252.18 E-value: 1.58e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 25 TFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALL-------ETPQRLFALV 97
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLsrpaladRKPEDPRALI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 98 LTPTRELAFQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKGFNLRALKYLVMDEAD 177
Cdd:PRK04537 90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVLDEAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 178 RILNMDFETEVDKILKVIPR--DRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYLFIPSKFKDTYLV 255
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 256 YILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVV 335
Cdd:PRK04537 250 GLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 336 VNFDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIEHLIGKKLPVFPTQDEEVMML--TERVNEAQRFARME 413
Cdd:PRK04537 330 YNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEPVTAELLTPLprPPRVPVEGEEADDE 409
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 26345792 414 LREH-GEKKKRKREDAGDDDDKEGaiGVRNKVAGGKMKKRKGR 455
Cdd:PRK04537 410 AGDSvGTIFREAREQRAAEEQRRG--GGRSGPGGGSRSGSVGG 450
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
35-225 |
1.20e-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: 237.54 E-value: 1.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 35 LCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLF---ALVLTPTRELAFQISEQ 111
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAatrVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 112 FEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDFETEVDKI 191
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....
gi 26345792 192 LKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVK 225
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVR 194
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
25-387 |
6.19e-76 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 244.72 E-value: 6.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 25 TFKDLGVT-DVLCEACDQlGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQR------LFALV 97
Cdd:PRK10590 2 SFDSLGLSpDILRAVAEQ-GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 98 LTPTRELAFQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDhLENTKGFNLRALKYLVMDEAD 177
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 178 RILNMDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYLFIPSKFKDTYLVYI 257
Cdd:PRK10590 160 RMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 258 LNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVN 337
Cdd:PRK10590 240 IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 26345792 338 FDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIEHLIGKKLP 387
Cdd:PRK10590 320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIP 369
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
19-386 |
1.79e-73 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 238.66 E-value: 1.79e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 19 EEEETKT-FKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETP---QRLF 94
Cdd:PRK01297 81 EPQEGKTrFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPppkERYM 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 95 ----ALVLTPTRELAFQISEQFEALGSSIGVQCAVIVGGIDSMSQSLAL-AKKPHIVIATPGRLIDHLENtKGFNLRALK 169
Cdd:PRK01297 161 geprALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQR-GEVHLDMVE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 170 YLVMDEADRILNMDFETEVDKILKVIPR--DRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYLFIPS 247
Cdd:PRK01297 240 VMVLDEADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAVAG 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 248 KFKDTYLVYILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGL 327
Cdd:PRK01297 320 SDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGI 399
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 26345792 328 DIPHVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIEHLIGKKL 386
Cdd:PRK01297 400 HIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKI 458
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
4-398 |
1.73e-67 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 220.85 E-value: 1.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 4 DEEPDSPSGALQTAAE---EEETKTFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAF-- 78
Cdd:PTZ00424 5 EQKNQSEQVASTGTIEsnyDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFvi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 79 -ALPILNALLETPQrlfALVLTPTRELAFQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHL 157
Cdd:PTZ00424 85 aALQLIDYDLNACQ---ALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 158 ENtKGFNLRALKYLVMDEADRILNMDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEK 237
Cdd:PTZ00424 162 DK-RHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 238 LQQYYLFIPS-KFKDTYLVYILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSI 316
Cdd:PTZ00424 241 IRQFYVAVEKeEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 317 LLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIEHLigkklpvFPTQDEEV 396
Cdd:PTZ00424 321 LITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIERH-------YNTQIEEM 393
|
..
gi 26345792 397 MM 398
Cdd:PTZ00424 394 PM 395
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
23-388 |
5.28e-65 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 215.22 E-value: 5.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 23 TKTFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQ---------Rl 93
Cdd:PRK04837 7 EQKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPApedrkvnqpR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 94 fALVLTPTRELAFQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENtKGFNLRALKYLVM 173
Cdd:PRK04837 86 -ALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQ-NHINLGAIQVVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 174 DEADRILNMDFETEVDKILKVIP--RDRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQyYLFIPSK-FK 250
Cdd:PRK04837 164 DEADRMFDLGFIKDIRWLFRRMPpaNQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKE-ELFYPSNeEK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 251 DTYLVYILNELAGNSFMIFCST---CNNT--------QRTALLLrnlgftaiplhGQMSQSKRLGSLNKFKAKARSILLA 319
Cdd:PRK04837 243 MRLLQTLIEEEWPDRAIIFANTkhrCEEIwghlaadgHRVGLLT-----------GDVAQKKRLRILEEFTRGDLDILVA 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 320 TDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITFV-TQYDVELfQRIEHLIGKKLPV 388
Cdd:PRK04837 312 TDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLAcEEYALNL-PAIETYIGHSIPV 380
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
35-224 |
6.55e-65 |
|
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: 208.33 E-value: 6.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 35 LCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRL--------FALVLTPTRELAF 106
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeetkddgpYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 107 QISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENtKGFNLRALKYLVMDEADRILNMDFET 186
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLER-RLLVLNQCTYVVLDEADRMIDMGFEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 26345792 187 EVDKILKVIP--------------------RDRKTFLFSATMTKKVQKLQRAALKNPV 224
Cdd:cd17945 160 QVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPV 217
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
33-224 |
6.29e-62 |
|
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: 200.12 E-value: 6.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 33 DVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLE------TPQRLFALVLTPTRELAF 106
Cdd:cd17961 3 PRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKakaesgEEQGTRALILVPTRELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 107 QISEQFEALGSSIG--VQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDF 184
Cdd:cd17961 83 QVSKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLSYGY 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 26345792 185 ETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPV 224
Cdd:cd17961 163 EEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
25-222 |
7.51e-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: 200.41 E-value: 7.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 25 TFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRL----------F 94
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSvgrgrrkaypS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 95 ALVLTPTRELAFQISEQ---FeALGSsiGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKgFNLRALKYL 171
Cdd:cd17967 81 ALILAPTRELAIQIYEEarkF-SYRS--GVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGR-ISLSSIKFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 26345792 172 VMDEADRILNMDFETEVDKILK----VIPRDRKTFLFSATMTKKVQKLQRAALKN 222
Cdd:cd17967 157 VLDEADRMLDMGFEPQIRKIVEhpdmPPKGERQTLMFSATFPREIQRLAADFLKN 211
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
48-215 |
2.94e-61 |
|
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: 196.69 E-value: 2.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 48 TKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELAFQISEQFEALGSSIGVQCAVIV 127
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 128 GGiDSMSQSLALAKKPHIVIATPGRLIDHLENTKgfNLRALKYLVMDEADRILNMDFETEVDKILKVIPRDRKTFLFSAT 207
Cdd:pfam00270 81 GG-DSRKEQLEKLKGPDILVGTPGRLLDLLQERK--LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157
|
....*...
gi 26345792 208 MTKKVQKL 215
Cdd:pfam00270 158 LPRNLEDL 165
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
41-225 |
2.30e-59 |
|
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: 192.97 E-value: 2.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 41 QLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPIL-----NALLETPQRLFALVLTPTRELAFQISEQFEAL 115
Cdd:cd17966 7 RQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvhinaQPPLERGDGPIVLVLAPTRELAQQIQQEANKF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 116 GSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKGfNLRALKYLVMDEADRILNMDFETEVDKILKVI 195
Cdd:cd17966 87 GGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKT-NLRRVTYLVLDEADRMLDMGFEPQIRKIVDQI 165
|
170 180 190
....*....|....*....|....*....|
gi 26345792 196 PRDRKTFLFSATMTKKVQKLQRAALKNPVK 225
Cdd:cd17966 166 RPDRQTLMWSATWPKEVRRLAEDFLKDYIQ 195
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
238-367 |
1.78e-58 |
|
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: 188.10 E-value: 1.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 238 LQQYYLFIPSKFKDTYL-VYILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSI 316
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 26345792 317 LLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITFV 367
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
43-224 |
8.98e-58 |
|
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: 189.04 E-value: 8.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 43 GWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLE---TPQR-LFALVLTPTRELAFQISEQFEALGSS 118
Cdd:cd17941 9 GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRerwTPEDgLGALIISPTRELAMQIFEVLRKVGKY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 119 IGVQCAVIVGGIDSMSQSLALAKKpHIVIATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDFETEVDKILKVIPRD 198
Cdd:cd17941 89 HSFSAGLIIGGKDVKEEKERINRM-NILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDAIVENLPKS 167
|
170 180
....*....|....*....|....*.
gi 26345792 199 RKTFLFSATMTKKVQKLQRAALKNPV 224
Cdd:cd17941 168 RQTLLFSATQTKSVKDLARLSLKNPE 193
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
25-226 |
1.06e-57 |
|
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: 189.05 E-value: 1.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 25 TFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQR--LFALVLTPTR 102
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTvgARALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 103 ELAFQISEQFEALGSSIGVQCAVIVGGiDSM-SQSLALAKKPHIVIATPGRLIDHLENTkGFNLRALKYLVMDEADRILN 181
Cdd:cd17959 82 ELALQTLKVTKELGKFTDLRTALLVGG-DSLeEQFEALASNPDIIIATPGRLLHLLVEM-NLKLSSVEYVVFDEADRLFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 26345792 182 MDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKC 226
Cdd:cd17959 160 MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
42-239 |
3.86e-56 |
|
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: 185.91 E-value: 3.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 42 LGWAKPTKIQIEAIPLAL-QGRDIIGLAETGSGKTGAFALPILNALLE--------TPQR-LFALVLTPTRELAFQISEQ 111
Cdd:cd17946 8 LGFSEPTPIQALALPAAIrDGKDVIGAAETGSGKTLAFGIPILERLLSqkssngvgGKQKpLRALILTPTRELAVQVKDH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 112 FEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKGF--NLRALKYLVMDEADRIL-NMDFEtEV 188
Cdd:cd17946 88 LKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHlaNLKSLRFLVLDEADRMLeKGHFA-EL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 26345792 189 DKILKVIPRD-------RKTFLFSATMTKKVQklQRAALKNPVKcavSSKYQTVEKLQ 239
Cdd:cd17946 167 EKILELLNKDragkkrkRQTFVFSATLTLDHQ--LPLKLNSKKK---KKKKEKKQKLE 219
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
38-223 |
1.96e-55 |
|
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: 182.95 E-value: 1.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 38 ACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALP---ILNALLETPQR-LFALVLTPTRELAFQISEQFE 113
Cdd:cd17942 4 AIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPaieLLYKLKFKPRNgTGVIIISPTRELALQIYGVAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 114 ALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDFETEVDKILK 193
Cdd:cd17942 84 ELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQIIK 163
|
170 180 190
....*....|....*....|....*....|
gi 26345792 194 VIPRDRKTFLFSATMTKKVQKLQRAALKNP 223
Cdd:cd17942 164 LLPKRRQTMLFSATQTRKVEDLARISLKKK 193
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
42-224 |
1.14e-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: 181.24 E-value: 1.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 42 LGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRL------FALVLTPTRELAFQISEQFEAL 115
Cdd:cd17949 9 MGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVdrsdgtLALVLVPTRELALQIYEVLEKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 116 GS-SIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDFETEVDKILKV 194
Cdd:cd17949 89 LKpFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILEL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 26345792 195 I-------------PRDRKTFLFSATMTKKVQKLQRAALKNPV 224
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) ... |
24-226 |
2.98e-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: 180.65 E-value: 2.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 24 KTFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETP-----QRLFALVL 98
Cdd:cd17953 12 QKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRpvkpgEGPIGLIM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 99 TPTRELAFQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHL--ENTKGFNLRALKYLVMDEA 176
Cdd:cd17953 92 APTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVTNLRRVTYVVLDEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 26345792 177 DRILNMDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKC 226
Cdd:cd17953 172 DRMFDMGFEPQIMKIVNNIRPDRQTVLFSATFPRKVEALARKVLHKPIEI 221
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
46-224 |
1.23e-53 |
|
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: 178.30 E-value: 1.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 46 KPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRL--------FALVLTPTRELA---FQISEQF-E 113
Cdd:cd17951 12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLpfikgegpYGLIVCPSRELArqtHEVIEYYcK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 114 AL--GSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLeNTKGFNLRALKYLVMDEADRILNMDFETEVDKI 191
Cdd:cd17951 92 ALqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDML-NKKKINLDICRYLCLDEADRMIDMGFEEDIRTI 170
|
170 180 190
....*....|....*....|....*....|...
gi 26345792 192 LKVIPRDRKTFLFSATMTKKVQKLQRAALKNPV 224
Cdd:cd17951 171 FSYFKGQRQTLLFSATMPKKIQNFAKSALVKPV 203
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
25-376 |
1.88e-53 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 186.92 E-value: 1.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 25 TFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNAL-------LETPQRLFALV 97
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCctirsghPSEQRNPLAMV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 98 LTPTRELAFQISEQFEALGSSIGVQCAVIVGGiDSMSQSLALAKKP-HIVIATPGRLIDHLeNTKGFNLRALKYLVMDEA 176
Cdd:PLN00206 202 LTPTRELCVQVEDQAKVLGKGLPFKTALVVGG-DAMPQQLYRIQQGvELIVGTPGRLIDLL-SKHDIELDNVSVLVLDEV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 177 DRILNMDFETEVDKILKVIPRDrKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYLFIPSKFKDTYLVY 256
Cdd:PLN00206 280 DCMLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFD 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 257 ILneLAGNSFMIFCSTCNNTQRTALLLRN-----LGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPH 331
Cdd:PLN00206 359 IL--KSKQHFKPPAVVFVSSRLGADLLANaitvvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLR 436
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 26345792 332 VDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQ 376
Cdd:PLN00206 437 VRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFP 481
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
31-221 |
1.32e-52 |
|
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: 175.85 E-value: 1.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 31 VTDVLCEACDQLGWAKPTKIQIEAIPLALQ-GRDIIGLAETGSGKTGAFALPILNALLETPQRL-----FALVLTPTREL 104
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGrrsgvSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 105 AFQISEQFEAL---GSSIGVQCAVivGGIDSMSQSLALAK-KPHIVIATPGRLIDHLENTKGFN-LRALKYLVMDEADRI 179
Cdd:cd17964 81 ALQIAAEAKKLlqgLRKLRVQSAV--GGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVAKaFTDLDYLVLDEADRL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 26345792 180 LNMDFETEVDKILKVIP----RDRKTFLFSATMTKKVQKLQRAALK 221
Cdd:cd17964 159 LDMGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTLK 204
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
35-225 |
1.50e-52 |
|
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: 175.30 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 35 LCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRL-----FALVLTPTRELAFQIS 109
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEkgegpIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 110 EQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLEnTKGFNLRALKYLVMDEADRILNMDFETEVD 189
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVK-KKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 26345792 190 KILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVK 225
Cdd:cd17952 160 SIVGHVRPDRQTLLFSATFKKKIEQLARDILSDPIR 195
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
37-225 |
1.64e-51 |
|
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: 172.76 E-value: 1.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 37 EACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALL-----ETPQRLFALVLTPTRELAFQISEQ 111
Cdd:cd17960 3 DVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLkrkanLKKGQVGALIISPTRELATQIYEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 112 FEALGSSIG--VQCAVIVGGIDSMSQSLAL-AKKPHIVIATPGRLIDHLENTKG-FNLRALKYLVMDEADRILNMDFETE 187
Cdd:cd17960 83 LQSFLEHHLpkLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRKADkVKVKSLEVLVLDEADRLLDLGFEAD 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 26345792 188 VDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVK 225
Cdd:cd17960 163 LNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVR 200
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
41-241 |
1.91e-51 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 172.68 E-value: 1.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 41 QLGWAKPTKIQIEAIPLALQG-RDIIGLAETGSGKTGAFALPILNALLETPQRlFALVLTPTRELAFQISEQFEALGSSI 119
Cdd:smart00487 3 KFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGG-RVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 120 GVQCAVIVGGIDSMSQSLALAK-KPHIVIATPGRLIDHLENtKGFNLRALKYLVMDEADRILNMDFETEVDKILKVIPRD 198
Cdd:smart00487 82 GLKVVGLYGGDSKREQLRKLESgKTDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 26345792 199 RKTFLFSATMTKKVQKLQRAALKNPVKcaVSSKYQTVEKLQQY 241
Cdd:smart00487 161 VQLLLLSATPPEEIENLLELFLNDPVF--IDVGFTPLEPIEQF 201
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
26-225 |
2.40e-50 |
|
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: 169.79 E-value: 2.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 26 FKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELA 105
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 106 FQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDhLENTKGFNLRALKYLVMDEADRILNMDFE 185
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILD-LAKKGVADLSHCKTLVLDEADKLLSQDFQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 26345792 186 TEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVK 225
Cdd:cd17940 160 PIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYE 199
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
43-228 |
1.08e-49 |
|
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: 167.77 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 43 GWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQR--LFALVLTPTRELAFQISEQFEALGSSIG 120
Cdd:cd17957 9 GYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKkgLRALILAPTRELASQIYRELLKLSKGTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 121 VQCAVIVGGI-DSMSQSLALAKKPHIVIATPGRLIDHLENTKgFNLRALKYLVMDEADRILNMDFETEVDKILKVI--PR 197
Cdd:cd17957 89 LRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQGP-IDLSSVEYLVLDEADKLFEPGFREQTDEILAACtnPN 167
|
170 180 190
....*....|....*....|....*....|.
gi 26345792 198 DRKTFlFSATMTKKVQKLQRAALKNPVKCAV 228
Cdd:cd17957 168 LQRSL-FSATIPSEVEELARSVMKDPIRIIV 197
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
25-221 |
5.94e-49 |
|
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: 168.22 E-value: 5.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 25 TFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLET---------PQRLFA 95
Cdd:cd18052 44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgltassfseVQEPQA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 96 LVLTPTRELAFQIseQFEALGSSIG--VQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKgFNLRALKYLVM 173
Cdd:cd18052 124 LIVAPTRELANQI--FLEARKFSYGtcIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGK-ISLSKLKYLIL 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 26345792 174 DEADRILNMDFETEVDKILKV--IPR--DRKTFLFSATMTKKVQKLQRAALK 221
Cdd:cd18052 201 DEADRMLDMGFGPEIRKLVSEpgMPSkeDRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
26-224 |
1.36e-46 |
|
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: 159.79 E-value: 1.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 26 FKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILnalletpQRLFALVLTPTRELA 105
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-------QIVVALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 106 FQISEQFEALGSSI---GVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKgFNLRALKYLVMDEADRILNM 182
Cdd:cd17938 74 EQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGK-LDLSSVRFFVLDEADRLLSQ 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 26345792 183 DFETEVDKILKVIPR-----DR-KTFLFSATM-TKKVQKLQRAALKNPV 224
Cdd:cd17938 153 GNLETINRIYNRIPKitsdgKRlQVIVCSATLhSFEVKKLADKIMHFPT 201
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
43-225 |
3.25e-46 |
|
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: 158.64 E-value: 3.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 43 GWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELAFQISEQFEALGSSIGVQ 122
Cdd:cd17939 16 GFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQIQKVVKALGDYMGVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 123 CAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLeNTKGFNLRALKYLVMDEADRILNMDFETEVDKILKVIPRDRKTF 202
Cdd:cd17939 96 VHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDML-QRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPPETQVV 174
|
170 180
....*....|....*....|...
gi 26345792 203 LFSATMTKKVQKLQRAALKNPVK 225
Cdd:cd17939 175 LFSATMPHEVLEVTKKFMRDPVR 197
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
37-224 |
6.24e-46 |
|
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: 158.01 E-value: 6.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 37 EACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETP----QRL--FALVLTPTRELAFQISE 110
Cdd:cd17958 3 KEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPipreQRNgpGVLVLTPTRELALQIEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 111 QFEALgSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDhLENTKGFNLRALKYLVMDEADRILNMDFETEVDK 190
Cdd:cd17958 83 ECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 26345792 191 ILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPV 224
Cdd:cd17958 161 ILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPM 194
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
25-228 |
8.51e-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: 159.44 E-value: 8.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 25 TFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLET--------------- 89
Cdd:cd18051 22 TFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIYEQgpgeslpsesgyygr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 90 -PQRLFALVLTPTRELAFQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKgFNLRAL 168
Cdd:cd18051 102 rKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPGRLVDMLERGK-IGLDYC 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26345792 169 KYLVMDEADRILNMDFETEVDKILK--VIPR--DRKTFLFSATMTKKVQKLQRAALKNPVKCAV 228
Cdd:cd18051 181 KYLVLDEADRMLDMGFEPQIRRIVEqdTMPPtgERQTLMFSATFPKEIQMLARDFLDNYIFLAV 244
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
35-223 |
1.79e-45 |
|
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: 157.79 E-value: 1.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 35 LCEACDQLGWAKPTKIQIEAIPLALQG---------RDIIGLAETGSGKTGAFALPILNALLETP-QRLFALVLTPTREL 104
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVvPRLRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 105 AFQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPH--------IVIATPGRLIDHLENTKGFNLRALKYLVMDEA 176
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNSTPGFTLKHLRFLVIDEA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26345792 177 DRILNMDFETEVDKILKVIPRDRKT--------------------FLFSATMTKKVQKLQRAALKNP 223
Cdd:cd17956 161 DRLLNQSFQDWLETVMKALGRPTAPdlgsfgdanllersvrplqkLLFSATLTRDPEKLSSLKLHRP 227
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
43-225 |
8.40e-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: 152.32 E-value: 8.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 43 GWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELAFQISEQFEALGSSI-GV 121
Cdd:cd17962 9 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMKGLpPM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 122 QCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLeNTKGFNLRALKYLVMDEADRILNMDFETEVDKILKVIPRDRKT 201
Cdd:cd17962 89 KTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDIL-KQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHDHQT 167
|
170 180
....*....|....*....|....
gi 26345792 202 FLFSATMTKKVQKLQRAALKNPVK 225
Cdd:cd17962 168 ILVSATIPRGIEQLAGQLLQNPVR 191
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
31-228 |
2.37e-41 |
|
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: 148.24 E-value: 2.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 31 VTDVLCeacdQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPIL-----NALLETPQRLFALVLTPTRELA 105
Cdd:cd18050 73 VMDVLL----DQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIvhinhQPYLERGDGPICLVLAPTRELA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 106 FQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKGfNLRALKYLVMDEADRILNMDFE 185
Cdd:cd18050 149 QQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRMLDMGFE 227
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 26345792 186 TEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCAV 228
Cdd:cd18050 228 PQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
26-224 |
1.12e-40 |
|
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350708 [Multi-domain] Cd Length: 208 Bit Score: 144.41 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 26 FKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELA 105
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 106 FQISEQFEALGSSI-GVQCAVIVGGIDSMSQSLALAKK-PHIVIATPGRLIDHLENtKGFNLRALKYLVMDEADRIL-NM 182
Cdd:cd17950 84 FQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKNKcPHIVVGTPGRILALVRE-KKLKLSHVKHFVLDECDKMLeQL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 26345792 183 DFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPV 224
Cdd:cd17950 163 DMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPL 204
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
44-230 |
1.29e-40 |
|
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: 145.15 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 44 WAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPIL-----NALLETPQRLFALVLTPTRELAFQISEQFEALGSS 118
Cdd:cd18049 44 FTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIvhinhQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 119 IGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKGfNLRALKYLVMDEADRILNMDFETEVDKILKVIPRD 198
Cdd:cd18049 124 CRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPD 202
|
170 180 190
....*....|....*....|....*....|..
gi 26345792 199 RKTFLFSATMTKKVQKLQRAALKNPVKCAVSS 230
Cdd:cd18049 203 RQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
43-207 |
2.89e-37 |
|
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: 134.70 E-value: 2.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 43 GWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELAFQISEQFEALGSSI-GV 121
Cdd:cd17943 9 GFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKKIGKKLeGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 122 QCAVIVGGIDsMSQSLALAKKPHIVIATPGRlIDHLENTKGFNLRALKYLVMDEADRILNMDFETEVDKILKVIPRDRKT 201
Cdd:cd17943 89 KCEVFIGGTP-VKEDKKKLKGCHIAVGTPGR-IKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSSLPKNKQV 166
|
....*.
gi 26345792 202 FLFSAT 207
Cdd:cd17943 167 IAFSAT 172
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
42-225 |
6.82e-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: 133.85 E-value: 6.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 42 LGWAKPTKIQIEAIPLALQG--RDIIGLAETGSGKTGAFALPIL---NALLETPQrlfALVLTPTRELAFQISEQFEALG 116
Cdd:cd17963 12 MGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLsrvDPTLKSPQ---ALCLAPTRELARQIGEVVEKMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 117 SSIGVQCAVIVGGIDSMSQSLALAkkpHIVIATPGRLIDHLEnTKGFNLRALKYLVMDEADRILNMD-FETEVDKILKVI 195
Cdd:cd17963 89 KFTGVKVALAVPGNDVPRGKKITA---QIVIGTPGTVLDWLK-KRQLDLKKIKILVLDEADVMLDTQgHGDQSIRIKRML 164
|
170 180 190
....*....|....*....|....*....|
gi 26345792 196 PRDRKTFLFSATMTKKVQKLQRAALKNPVK 225
Cdd:cd17963 165 PRNCQILLFSATFPDSVRKFAEKIAPNANT 194
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
26-225 |
3.74e-36 |
|
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: 132.18 E-value: 3.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 26 FKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNAL---LETPQrlfALVLTPTR 102
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIdtsLKATQ---ALVLAPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 103 ELAFQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLeNTKGFNLRALKYLVMDEADRILNM 182
Cdd:cd18046 78 ELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMI-NRRYLRTDYIKMFVLDEADEMLSR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 26345792 183 DFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVK 225
Cdd:cd18046 157 GFKDQIYDIFQKLPPDTQVVLLSATMPNDVLEVTTKFMRDPIR 199
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
250-358 |
5.31e-33 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 120.39 E-value: 5.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 250 KDTYLVYILNELAGNSFMIFCSTCNNTQrTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDI 329
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 26345792 330 PHVDVVVNFDIPTHSKDYIHRVGRTARAG 358
Cdd:pfam00271 81 PDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
26-225 |
1.64e-32 |
|
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: 122.19 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 26 FKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELA 105
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 106 FQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENtKGFNLRALKYLVMDEADRILNMDFE 185
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADEMLNKGFK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 26345792 186 TEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVK 225
Cdd:cd18045 160 EQIYDVYRYLPPATQVVLVSATLPQDILEMTNKFMTDPIR 199
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
35-215 |
2.15e-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: 114.77 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 35 LCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALL---ETPQRLF----ALVLTPTRELAFQ 107
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLrykLLAEGPFnaprGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 108 ISEQFEALGSSIGVQCAVIVGGiDSMSQSLALA-KKPHIVIATPGrLIDHLENTKGFNLRALKYLVMDEADRILNMDFET 186
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGG-RTKRQIRNPHfEEVDILVATPG-ALSKLLTSRIYSLEQLRHLVLDEADTLLDDSFNE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 26345792 187 EVDKILK-----------VIPRDRKT--FLFSATMTKKVQKL 215
Cdd:cd17948 159 KLSHFLRrfplasrrsenTDGLDPGTqlVLVSATMPSGVGEV 200
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
50-221 |
3.07e-27 |
|
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: 108.01 E-value: 3.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 50 IQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLF------ALVLTPTRELAFQISEQFEALGSSIGVQC 123
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKrgrapkVLVLAPTRELANQVTKDFKDITRKLSVAC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 124 avIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKgFNLRALKYLVMDEADRILNMDFETEVDKILKVI----PRDR 199
Cdd:cd17944 96 --FYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGR-LDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSykkdSEDN 172
|
170 180
....*....|....*....|...
gi 26345792 200 -KTFLFSATMTKKVQKLQRAALK 221
Cdd:cd17944 173 pQTLLFSATCPDWVYNVAKKYMK 195
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
277-358 |
6.41e-27 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 103.06 E-value: 6.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 277 QRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTAR 356
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 26345792 357 AG 358
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
24-223 |
5.13e-21 |
|
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: 91.24 E-value: 5.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 24 KTFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQG--RDIIGLAETGSGKTGAFALPIL---NALLETPQrlfALVL 98
Cdd:cd18048 18 KSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLsrvDALKLYPQ---CLCL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 99 TPTRELAFQISEQFEALGS-SIGVQCAVIVGGiDSMSQSLALAKKphIVIATPGRLIDHLENTKGFNLRALKYLVMDEAD 177
Cdd:cd18048 95 SPTFELALQTGKVVEEMGKfCVGIQVIYAIRG-NRPGKGTDIEAQ--IVIGTPGTVLDWCFKLRLIDVTNISVFVLDEAD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 26345792 178 RILNMD-FETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNP 223
Cdd:cd18048 172 VMINVQgHSDHSVRVKRSMPKECQMLLFSATFEDSVWAFAERIVPDP 218
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
24-223 |
1.97e-19 |
|
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: 86.31 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 24 KTFKDLGVTDVLCEACDQLGWAKPTKIQIEAIPLALQG--RDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPT 101
Cdd:cd18047 1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 102 RELAFQISEQFEALGSSI-GVQCAVIVGGiDSMSQSLALakKPHIVIATPGRLIDHLENTKGFNLRALKYLVMDEAD-RI 179
Cdd:cd18047 81 YELALQTGKVIEQMGKFYpELKLAYAVRG-NKLERGQKI--SEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADvMI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 26345792 180 LNMDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNP 223
Cdd:cd18047 158 ATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDP 201
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
67-207 |
2.26e-19 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 84.38 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 67 LAETGSGKTGAFALPILNALLEtpQRLFALVLTPTRELAFQISEQFEALgSSIGVQCAVIVGGIDSMSQSLALAKKPHIV 146
Cdd:cd00046 7 TAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSSAEEREKNKLGDADII 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26345792 147 IATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDFETEVDK--ILKVIPRDRKTFLFSAT 207
Cdd:cd00046 84 IATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
51-435 |
6.70e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 83.15 E-value: 6.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 51 QIEAI-----PLALQGRDIIGLAETGSGKTGAFALpilnALLETPQRLFALVLTPTRELAFQISEQFEAL-------GSS 118
Cdd:COG1061 85 QQEALeallaALERGGGRGLVVAPTGTGKTVLALA----LAAELLRGKRVLVLVPRRELLEQWAEELRRFlgdplagGGK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 119 IGVQCAVIVGGIDSmsqslaLAKKPHIviatpgrliDHLENTKGfnlralkYLVMDEADRILNMDFEtevdkilKVIPRD 198
Cdd:COG1061 161 KDSDAPITVATYQS------LARRAHL---------DELGDRFG-------LVIIDEAHHAGAPSYR-------RILEAF 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 199 RKTFL--FSAT------------------MTKKVQKLQRAALKNPVKC--------AVSSKYQTVEKLQQYYLFIPSKFK 250
Cdd:COG1061 212 PAAYRlgLTATpfrsdgreillflfdgivYEYSLKEAIEDGYLAPPEYygirvdltDERAEYDALSERLREALAADAERK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 251 DTYLVYILNELAGNSF-MIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDI 329
Cdd:COG1061 292 DKILRELLREHPDDRKtLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDV 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 330 PHVDVVVNFDiPTHSK-DYIHRVGRTARAGRSGKAITFVTQYDV------ELFQRIEHLIGKKLPVFPTQDEEVMMLTER 402
Cdd:COG1061 372 PRLDVAILLR-PTGSPrEFIQRLGRGLRPAPGKEDALVYDFVGNdvpvleELAKDLRDLAGYRVEFLDEEESEELALLIA 450
|
410 420 430
....*....|....*....|....*....|...
gi 26345792 403 VNEAQRFARMELREHGEKKKRKREDAGDDDDKE 435
Cdd:COG1061 451 VKPALEVKGELEEELLEELELLEDALLLVLAEL 483
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
41-217 |
5.59e-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: 77.42 E-value: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 41 QLGWAKPTKIQIEAIPLALQ---------------GRDIIGLA-ETGSGKTGAFALPILNALLETPQRLF---------- 94
Cdd:cd17965 25 TDEEIKPSPIQTLAIKKLLKtlmrkvtkqtsneepKLEVFLLAaETGSGKTLAYLAPLLDYLKRQEQEPFeeaeeeyesa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 95 -------ALVLTPTRELAFQISEQFEALGSSIGVQCAVIVGGIDSMSQSLALA--KKPHIVIATPGrLIDHLENTKGFNL 165
Cdd:cd17965 105 kdtgrprSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQRLQLAfkGRIDILVTTPG-KLASLAKSRPKIL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 26345792 166 RALKYLVMDEADRILNMDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQR 217
Cdd:cd17965 184 SRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLR 235
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
35-176 |
1.76e-15 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 79.11 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 35 LCEACDQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPqRLFALVLTPTRELAF-Q---ISE 110
Cdd:COG1205 45 LRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP-GATALYLYPTKALARdQlrrLRE 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26345792 111 QFEALGssIGVQCAVIVGGIdSMSQSLALAKKPHIVIATP-----GrLIDHLENTKGFnLRALKYLVMDEA 176
Cdd:COG1205 124 LAEALG--LGVRVATYDGDT-PPEERRWIREHPDIVLTNPdmlhyG-LLPHHTRWARF-FRNLRYVVIDEA 189
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
51-176 |
4.56e-13 |
|
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: 67.22 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 51 QIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLfALVLTPTRELAFQISEQFEALGSSI--GVQCAVIVG 128
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSR-ALYLYPTKALAQDQLRSLRELLEQLglGIRVATYDG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 26345792 129 GIDSMSQSLALAKKPHIVIATPGRL---IDHLENTKGFNLRALKYLVMDEA 176
Cdd:cd17923 84 DTPREERRAIIRNPPRILLTNPDMLhyaLLPHHDRWARFLRNLRYVVLDEA 134
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
283-368 |
8.85e-12 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 67.45 E-value: 8.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 283 LRNLGFTAIPLHGQ--------MSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFD-IPTHSKdYIHRVGR 353
Cdd:COG1111 373 LSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpVPSEIR-SIQRKGR 451
|
90
....*....|....*
gi 26345792 354 TARaGRSGKAITFVT 368
Cdd:COG1111 452 TGR-KREGRVVVLIA 465
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
48-176 |
2.09e-11 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 62.66 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 48 TKIQIEAIPLALQGRDIIGL-AETGSGKTGAFALPILNALLETPQRlfALVLTPTRELAFQISEQFEALGSSIGVQCAVI 126
Cdd:cd17921 3 NPIQREALRALYLSGDSVLVsAPTSSGKTLIAELAILRALATSGGK--AVYIAPTRALVNQKEADLRERFGPLGKNVGLL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 26345792 127 VGGIDSMSQSLAlakKPHIVIATPGRLIDHLENTKGFNLRALKYLVMDEA 176
Cdd:cd17921 81 TGDPSVNKLLLA---EADILVATPEKLDLLLRNGGERLIQDVRLVVVDEA 127
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
61-175 |
9.04e-10 |
|
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: 57.59 E-value: 9.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 61 GRDIIGLAETGSGKTGAFALPILNALL-ETPQRLFALVLTPTRELAFQISEQFEALGSSIGVQCAVIV--GGIDSMSQSL 137
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLAdEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLEIPVAVrhGDTSQSEKAK 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 26345792 138 ALAKKPHIVIATPGRLIDHLENTKGFN-LRALKYLVMDE 175
Cdd:cd17922 81 QLKNPPGILITTPESLELLLVNKKLRElFAGLRYVVVDE 119
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
315-367 |
1.03e-09 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 54.63 E-value: 1.03e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 26345792 315 SILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAG-RSGKAITFV 367
Cdd:cd18785 24 EILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
282-369 |
1.25e-09 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 60.66 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 282 LLRNLGFTAIPLHGQ--------MSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFD-IPTHSKdYIHRVG 352
Cdd:PRK13766 384 LLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIR-SIQRKG 462
|
90
....*....|....*..
gi 26345792 353 RTARaGRSGKAITFVTQ 369
Cdd:PRK13766 463 RTGR-QEEGRVVVLIAK 478
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
296-357 |
3.52e-09 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 55.29 E-value: 3.52e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26345792 296 QMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRtARA 357
Cdd:cd18802 73 LMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
43-224 |
3.60e-09 |
|
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: 56.39 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 43 GWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPilnALLETPqrlFALVLTPTRELafqISEQFEALgSSIGVQ 122
Cdd:cd17920 9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLP---ALLLDG---VTLVVSPLISL---MQDQVDRL-QQLGIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 123 CAVIVGGIDSMSQSLALAK----KPHIVIATPGRL--------IDHLENTKGFNLralkyLVMDEADRILN--MDFETEV 188
Cdd:cd17920 79 AAALNSTLSPEEKREVLLRikngQYKLLYVTPERLlspdflelLQRLPERKRLAL-----IVVDEAHCVSQwgHDFRPDY 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 26345792 189 DKILKVIPRDRKT--FLFSATMTKKVQK--LQRAALKNPV 224
Cdd:cd17920 154 LRLGRLRRALPGVpiLALTATATPEVREdiLKRLGLRNPV 193
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
46-176 |
4.93e-09 |
|
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: 56.12 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 46 KPTKIQIEAIPLALQgRDIIGLAETGSGKTGAFALPI-----LNALLETPQRlFALVLTPTRELAFQiseQFEALGSSIG 120
Cdd:cd18034 2 TPRSYQLELFEAALK-RNTIVVLPTGSGKTLIAVMLIkemgeLNRKEKNPKK-RAVFLVPTVPLVAQ---QAEAIRSHTD 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 121 VQCAVIVGGIDSMSQS----LALAKKPHIVIATPGRLIDHLENTKgFNLRALKYLVMDEA 176
Cdd:cd18034 77 LKVGEYSGEMGVDKWTkerwKEELEKYDVLVMTAQILLDALRHGF-LSLSDINLLIFDEC 135
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
204-387 |
1.36e-08 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 56.69 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 204 FSATMTKKVQK--LQRAALKNPvKCAVSS------KYQTVEKLQQYylfipskfKDTYLVYILNELAGNSFMIFCSTCNN 275
Cdd:COG0514 172 LTATATPRVRAdiAEQLGLEDP-RVFVGSfdrpnlRLEVVPKPPDD--------KLAQLLDFLKEHPGGSGIVYCLSRKK 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 276 TQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATdVA-SRGLDIPHVDVVVNFDIPTHSKDYIHRVGRT 354
Cdd:COG0514 243 VEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRA 321
|
170 180 190
....*....|....*....|....*....|...
gi 26345792 355 ARAGRSGKAITFVTQYDVelfQRIEHLIGKKLP 387
Cdd:COG0514 322 GRDGLPAEALLLYGPEDV---AIQRFFIEQSPP 351
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
297-364 |
1.98e-08 |
|
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: 53.13 E-value: 1.98e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26345792 297 MSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARaGRSGKAI 364
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVV 140
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
51-377 |
3.30e-08 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 55.87 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 51 QIEAIPLALQGRDIIGLAETGSGKTGAFALP--ILNALletpqrlfALVLTPTRELAFQISEQFEALGSSigvqcAVIVG 128
Cdd:PRK11057 30 QQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPalVLDGL--------TLVVSPLISLMKDQVDQLLANGVA-----AACLN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 129 GIDSMSQSLALAKKPH-----IVIATPGRL-----IDHLENTKgfnlraLKYLVMDEADRI--LNMDFETEVDKILKVIP 196
Cdd:PRK11057 97 STQTREQQLEVMAGCRtgqikLLYIAPERLmmdnfLEHLAHWN------PALLAVDEAHCIsqWGHDFRPEYAALGQLRQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 197 R--DRKTFLFSATMTKKVQK--LQRAALKNPVkCAVSS------KYQTVEK---LQQYYLFIPSKfkdtylvyilnelAG 263
Cdd:PRK11057 171 RfpTLPFMALTATADDTTRQdiVRLLGLNDPL-IQISSfdrpniRYTLVEKfkpLDQLMRYVQEQ-------------RG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 264 NSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTH 343
Cdd:PRK11057 237 KSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRN 316
|
330 340 350
....*....|....*....|....*....|....
gi 26345792 344 SKDYIHRVGRTARAGRSGKAITFVTQYDVELFQR 377
Cdd:PRK11057 317 IESYYQETGRAGRDGLPAEAMLFYDPADMAWLRR 350
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
48-150 |
6.95e-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: 52.74 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 48 TKIQIEAIPLALQG-RDIIGLAETGSGKTGAFALPILNALLETPQ----RLFALVLTPTRELAFQISEQFEALGSSIGVQ 122
Cdd:cd18023 3 NRIQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERNPlpwgNRKVVYIAPIKALCSEKYDDWKEKFGPLGLS 82
|
90 100
....*....|....*....|....*...
gi 26345792 123 CAVIVGgiDSMSQSLALAKKPHIVIATP 150
Cdd:cd18023 83 CAELTG--DTEMDDTFEIQDADIILTTP 108
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
44-175 |
7.42e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 54.72 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 44 WAKPTKIQIEAIPLALQGRDIIGLAETGSGKT-GAFaLPILNALLETP------QRLFALVLTPTRELAFQISEQFEALG 116
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPrpgelpDGLRVLYISPLKALANDIERNLRAPL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26345792 117 SSIGVQCAVIVGGI-------D-SMSQSLALAKK-PHIVIATPgrlidhlE------NTKGF--NLRALKYLVMDE 175
Cdd:COG1201 101 EEIGEAAGLPLPEIrvgvrtgDtPASERQRQRRRpPHILITTP-------EslalllTSPDAreLLRGVRTVIVDE 169
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
51-175 |
1.63e-07 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 51.18 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 51 QIEAI-PLALQGRDIIGLAETGSGKTGAFALPILNALLETPQrlfALVLTPTRELAFQISEQFEALgSSIGVQCAVIVGG 129
Cdd:cd18028 6 QAEAVrAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGGK---ALYLVPLRALASEKYEEFKKL-EEIGLKVGISTGD 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 26345792 130 IDSMSQSLAlakKPHIVIATPGRLiDHLENTKGFNLRALKYLVMDE 175
Cdd:cd18028 82 YDEDDEWLG---DYDIIVATYEKF-DSLLRHSPSWLRDVGVVVVDE 123
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
68-381 |
3.65e-07 |
|
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: 52.05 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 68 AETGSGKTGAfALPILNALLETPQRLFALVLTPTRELAFQISEQFEALGSSIGVQCAVIVG-GIDSMSQSLALA------ 140
Cdd:cd09639 6 APTGYGKTEA-ALLWALHSLKSQKADRVIIALPTRATINAMYRRAKEAFGETGLYHSSILSsRIKEMGDSEEFEhlfply 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 141 -KKPHIVIATPGRL--IDHL--ENTKGFNLR-------ALKYLVMDEADRIL---NMDFETevdkILKVIPR-DRKTFLF 204
Cdd:cd09639 85 iHSNDTLFLDPITVctIDQVlkSVFGEFGHYeftlasiANSLLIFDEVHFYDeytLALILA----VLEVLKDnDVPILLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 205 SATMTKKVQKLqraalkNPVKCAVSSKYQTVEKLQQYYLFI----PSKFKDTYLVYILNEL-AGNSFMIFCSTCNNTQRT 279
Cdd:cd09639 161 SATLPKFLKEY------AEKIGYVEENEPLDLKPNERAPFIkiesDKVGEISSLERLLEFIkKGGSVAIIVNTVDRAQEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 280 ALLLRNLG--FTAIPLHGQMSQSKRLGS----LNKFKAKARSILLATDVASRGLDIpHVDVVVNFDIPTHSkdYIHRVGR 353
Cdd:cd09639 235 YQQLKEKGpeEEIMLIHSRFTEKDRAKKeaelLLEFKKSEKFVIVATQVIEASLDI-SVDVMITELAPIDS--LIQRLGR 311
|
330 340 350
....*....|....*....|....*....|....*....
gi 26345792 354 TARAGRSGKAITFVTQ----------YDVELFQR-IEHL 381
Cdd:cd09639 312 LHRYGEKNGEEVYIITdapdgkgqkpYPYDLVERtIELL 350
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
51-207 |
5.24e-07 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 48.84 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 51 QIEAIPLALQ----GRDIIGLAeTGSGKTgAFALPILNALLETPqrlfALVLTPTRELAFQISEQFEALG--SSIGVQCA 124
Cdd:cd17926 5 QEEALEAWLAhknnRRGILVLP-TGSGKT-LTALALIAYLKELR----TLIVVPTDALLDQWKERFEDFLgdSSIGLIGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 125 VIVGGIDSMSqslalakkphIVIATPGRLIDHLENTKGFNLRALkYLVMDEADRILNMDFEtevdKILKvIPRDRKTFLF 204
Cdd:cd17926 79 GKKKDFDDAN----------VVVATYQSLSNLAEEEKDLFDQFG-LLIVDEAHHLPAKTFS----EILK-ELNAKYRLGL 142
|
...
gi 26345792 205 SAT 207
Cdd:cd17926 143 TAT 145
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
245-341 |
1.61e-06 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 47.09 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 245 IPSKFKdtYLVYILNELAGNS--FMIFcstcnnTQRTALL------LRNLGFTAIPLHGQMSQSKRLGSLNKFKA--KAR 314
Cdd:cd18793 9 VSGKLE--ALLELLEELREPGekVLIF------SQFTDTLdileeaLRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIR 80
|
90 100
....*....|....*....|....*..
gi 26345792 315 SILLATDVASRGLDIPHVDVVVNFDIP 341
Cdd:cd18793 81 VFLLSTKAGGVGLNLTAANRVILYDPW 107
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
267-356 |
1.70e-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: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 267 MIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGS---LNKFKAKARSILLATDVASRGLDIPHVDVVVnFDIPTH 343
Cdd:cd18799 10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaliLLFFGELKPPILVTVDLLTTGVDIPEVDNVV-FLRPTE 88
|
90
....*....|....
gi 26345792 344 SKD-YIHRVGRTAR 356
Cdd:cd18799 89 SRTlFLQMLGRGLR 102
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
51-382 |
2.33e-06 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 50.28 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 51 QIEAIPLALQGRDIIGLAETGSGKTGAFALPilnALLETPqrlFALVLTPTRELafqISEQFEALGSSiGVQCAVIVGGI 130
Cdd:PLN03137 465 QREIINATMSGYDVFVLMPTGGGKSLTYQLP---ALICPG---ITLVISPLVSL---IQDQIMNLLQA-NIPAASLSAGM 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 131 DSMSQSLALAK------KPHIVIATPGR------LIDHLENTKGFNLraLKYLVMDEADRI--LNMDFETEVDK--ILKV 194
Cdd:PLN03137 535 EWAEQLEILQElsseysKYKLLYVTPEKvaksdsLLRHLENLNSRGL--LARFVIDEAHCVsqWGHDFRPDYQGlgILKQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 195 IPRDRKTFLFSATMTKKVQKLQRAALkNPVKCAVSSkyQTVEKLQQYYLFIPSKFKdtYLVYILNELAGNSF----MIFC 270
Cdd:PLN03137 613 KFPNIPVLALTATATASVKEDVVQAL-GLVNCVVFR--QSFNRPNLWYSVVPKTKK--CLEDIDKFIKENHFdecgIIYC 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 271 STCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHR 350
Cdd:PLN03137 688 LSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQE 767
|
330 340 350
....*....|....*....|....*....|..
gi 26345792 351 VGRtarAGRSGKAITFVTQYDVELFQRIEHLI 382
Cdd:PLN03137 768 CGR---AGRDGQRSSCVLYYSYSDYIRVKHMI 796
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
48-175 |
8.08e-06 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 48.34 E-value: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 48 TKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALL------ETPQRLFALVLTPTRELA-----------FQISE 110
Cdd:PRK13767 34 TPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFrlgregELEDKVYCLYVSPLRALNndihrnleeplTEIRE 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26345792 111 QFEALGSSI-GVQCAVIVGGIDSMSQSLALAKKPHIVIATPGRL-IdhLENTKGFN--LRALKYLVMDE 175
Cdd:PRK13767 114 IAKERGEELpEIRVAIRTGDTSSYEKQKMLKKPPHILITTPESLaI--LLNSPKFRekLRTVKWVIVDE 180
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
51-221 |
2.58e-05 |
|
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: 45.20 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 51 QIEAIPLALQGRDIIGLAETGSGKTGAFALPilnALLeTPQrlFALVLTPTRELafqISEQFEALgSSIGVQCAVIVGGI 130
Cdd:cd18016 22 QLEAINAALLGEDCFVLMPTGGGKSLCYQLP---ACV-SPG--VTVVISPLRSL---IVDQVQKL-TSLDIPATYLTGDK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 131 ---DSMSQSLALAKKPHIV---------IATPGRLIDHLENTKGFNLraLKYLVMDEADRI--LNMDFETEVDKiLKVIp 196
Cdd:cd18016 92 tdaEATKIYLQLSKKDPIIkllyvtpekISASNRLISTLENLYERKL--LARFVIDEAHCVsqWGHDFRPDYKR-LNML- 167
|
170 180 190
....*....|....*....|....*....|.
gi 26345792 197 rdRKTF------LFSATMTKKVQKLQRAALK 221
Cdd:cd18016 168 --RQKFpsvpmmALTATATPRVQKDILNQLK 196
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
246-362 |
2.96e-05 |
|
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: 43.74 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 246 PSKFKDTYLVYILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATdVA-S 324
Cdd:cd18794 13 KKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT-VAfG 91
|
90 100 110
....*....|....*....|....*....|....*...
gi 26345792 325 RGLDIPHVDVVVNFDIPTHSKDYIHRVGrtaRAGRSGK 362
Cdd:cd18794 92 MGIDKPDVRFVIHYSLPKSMESYYQESG---RAGRDGL 126
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
31-214 |
4.35e-05 |
|
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: 44.28 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 31 VTDVLCEacdQLGWAKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPilnALLEtpqRLFALVLTPTRELafqISE 110
Cdd:cd18015 6 VKDTLKN---VFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLP---ALCS---DGFTLVVSPLISL---MED 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 111 QFEALGsSIGVQCAVIVGGIDSMSQSLALA---KKP---HIVIATP------GRLIDHLEntKGFNLRALKYLVMDEAD- 177
Cdd:cd18015 74 QLMALK-KLGISATMLNASSSKEHVKWVHAaltDKNselKLLYVTPekiaksKRFMSKLE--KAYNAGRLARIAIDEVHc 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 26345792 178 -RILNMDFETEVDK--ILKVIPRDRKTFLFSATMTKKVQK 214
Cdd:cd18015 151 cSQWGHDFRPDYKKlgILKRQFPNVPILGLTATATSKVLK 190
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
306-380 |
1.70e-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: 43.00 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 306 LNKFKAKARSILLATDVASRGLDIPHVD--VVVNFDIPTHSKDY---------IHRV-GRTARAGRSGKAI--TFVTQYD 371
Cdd:cd18804 137 LDQFERGEIDILIGTQMIAKGLDFPNVTlvGILNADSGLNSPDFraserafqlLTQVsGRAGRGDKPGKVIiqTYNPEHP 216
|
....*....
gi 26345792 372 veLFQRIEH 380
Cdd:cd18804 217 --LIQAAKE 223
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
254-386 |
1.93e-04 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 44.06 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 254 LVYILNEL--AGNSFMIFcstcnnTQRTALL------LRNLGFTAIPLHGQMSQSKRLGSLNKFKAK--ARSILLATDVA 323
Cdd:COG0553 538 LLELLEELlaEGEKVLVF------SQFTDTLdlleerLEERGIEYAYLHGGTSAEERDELVDRFQEGpeAPVFLISLKAG 611
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26345792 324 SRGLDIPHVDVVVNFDIP---------ThskDYIHRVGRTaragRSGKAITFVTQYDVElfQRIEHLIGKKL 386
Cdd:COG0553 612 GEGLNLTAADHVIHYDLWwnpaveeqaI---DRAHRIGQT----RDVQVYKLVAEGTIE--EKILELLEEKR 674
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
256-364 |
1.13e-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: 39.17 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 256 YILNELAGNSFMIFCSTCNNTQRTALLLRNLGF-----TAIPLH-GQMSQSKRLGSLNKFKAKARSILLATDVASRGLDI 329
Cdd:cd18796 31 VIFLLERHKSTLVFTNTRSQAERLAQRLRELCPdrvppDFIALHhGSLSRELREEVEAALKRGDLKVVVATSSLELGIDI 110
|
90 100 110
....*....|....*....|....*....|....*
gi 26345792 330 PHVDVVVNFDIPTHSKDYIHRVGrtaRAGRSGKAI 364
Cdd:cd18796 111 GDVDLVIQIGSPKSVARLLQRLG---RSGHRPGAA 142
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
51-179 |
1.82e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 38.81 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 51 QIEAI------PLALQGRDIIGLAeTGSGKTGAFALPILNALLETPQRLFaLVLTPTRELAFQISEQFEALGSSIGVQCA 124
Cdd:pfam04851 8 QIEAIenllesIKNGQKRGLIVMA-TGSGKTLTAAKLIARLFKKGPIKKV-LFLVPRKDLLEQALEEFKKFLPNYVEIGE 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 26345792 125 VIVGgiDSMSQSLALAKkphIVIATPGRLIDHLENTKGFNLR-ALKYLVMDEADRI 179
Cdd:pfam04851 86 IISG--DKKDESVDDNK---IVVTTIQSLYKALELASLELLPdFFDVIIIDEAHRS 136
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
51-178 |
2.24e-03 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 39.03 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 51 QIEAIPLALQGRDIIgLAETGSGKTgAFALPILNALLeTPQRLFALVLTPTRELAFQISEQFEALgSSIGVQCAVIVGGI 130
Cdd:cd18035 7 QVLIAAVALNGNTLI-VLPTGLGKT-IIAILVAADRL-TKKGGKVLILAPSRPLVEQHAENLKRV-LNIPDKITSLTGEV 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 26345792 131 DSMSQSlALAKKPHIVIATPGRLIDHLENTKgFNLRALKYLVMDEADR 178
Cdd:cd18035 83 KPEERA-ERWDASKIIVATPQVIENDLLAGR-ITLDDVSLLIFDEAHH 128
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
254-386 |
2.26e-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: 38.82 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 254 LVYILNELaGNSFMIFCSTCNNTQ---RTALLLRNLGFTAIPLHgqmsqSKRLGSLNKFKAkaRSILLATDVAS------ 324
Cdd:cd18798 16 LLELVKKL-GDGGLIFVSIDYGKEyaeELKEFLERHGIKAELAL-----SSTEKNLEKFEE--GEIDVLIGVASyygvlv 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26345792 325 RGLDIPH-VDVVVNFDIPTHSkdYIHRVGRTAR--AGRSGKAITFVTQYDVELFqrieHLIGKKL 386
Cdd:cd18798 88 RGIDLPErIKYAIFYGVPVTT--YIQASGRTSRlyAGGLTKGLSVVLVDDPELF----EALKKRL 146
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
46-178 |
3.76e-03 |
|
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: 38.57 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 46 KPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFA--LVLTPTRELAFQISEQFEALGSSIGVQC 123
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGkvVFLANKVPLVEQQKEVFRKHFERPGYKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 26345792 124 AVIVGGIDSMSQSLALAKKPHIVIATPGRLIDHLENTKGFNLRALKYLVMDEADR 178
Cdd:cd17927 82 TGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
48-329 |
5.19e-03 |
|
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; CRISPR-Cas type I system-associated endonuclease/helicase Cas3 is part of the Pathway/BioSystem: CRISPR-Cas system
Pssm-ID: 440816 [Multi-domain] Cd Length: 535 Bit Score: 39.29 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 48 TKIQIEAIPLALQGRDIIGL-AETGSGKTGAFALPILNALLET-PQRLF-ALvltPTRELAFQISEQFEALG-------- 116
Cdd:COG1203 133 NEALELALEAAEEEPGLFILtAPTGGGKTEAALLFALRLAAKHgGRRIIyAL---PFTSIINQTYDRLRDLFgedvllhh 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 117 SSIGVQCAVIVGGIDSMSQSLALAKK----PhIVIATPGRLIDHLENTKGFNLRAL-----KYLVMDEADrilnmDFETE 187
Cdd:COG1203 210 SLADLDLLEEEEEYESEARWLKLLKElwdaP-VVVTTIDQLFESLFSNRKGQERRLhnlanSVIILDEVQ-----AYPPY 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 188 ----VDKILKVIPRDRKTFLF-SATMTkkvqKLQRAALKNPVKCAVSSKYQTVEKLQQYY-----LFIPSKFKDTYLVYI 257
Cdd:COG1203 284 mlalLLRLLEWLKNLGGSVILmTATLP----PLLREELLEAYELIPDEPEELPEYFRAFVrkrveLKEGPLSDEELAELI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 258 LNELA-GNSFMIFCSTCNNTQRTALLLRNLGfTAIP---LHGQMSQSKRLGSLNK----FKAKARSILLATDVASRGLDI 329
Cdd:COG1203 360 LEALHkGKSVLVIVNTVKDAQELYEALKEKL-PDEEvylLHSRFCPADRSEIEKEikerLERGKPCILVSTQVVEAGVDI 438
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
293-358 |
5.69e-03 |
|
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: 37.63 E-value: 5.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345792 293 LHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIH----RVGRTARAG 358
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHqlrgRVGRGKHQS 135
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
293-363 |
9.42e-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: 36.55 E-value: 9.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26345792 293 LHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRV-GRTARAGRSGKA 363
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNANTIIIERADKFGLAQLYQLrGRVGRSKERAYA 128
|
|
| |
