|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
23-453 |
9.35e-158 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 452.68 E-value: 9.35e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 23 TKTFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQR-LFALVLTPT 101
Cdd:COG0513 1 MMSFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRaPQALILAPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 102 RELAFQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENtKGFNLRALKYLVMDEADRILN 181
Cdd:COG0513 81 RELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIER-GALDLSGVETLVLDEADRMLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 182 MDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYIFIPSKFKDTYLVYILNEL 261
Cdd:COG0513 160 MGFIEDIERILKLLPKERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLVDKRDKLELLRRLLRDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 262 AGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIP 341
Cdd:COG0513 240 DPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVINYDLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 342 THSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIEHLIGKKLPgfptqddEVMMLTERVAEAQRFARMElrehGEKK 421
Cdd:COG0513 320 EDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLIGQKIE-------EEELPGFEPVEEKRLERLK----PKIK 388
|
410 420 430
....*....|....*....|....*....|..
gi 52782792 422 KRSREDAGDNDDTEGAIGVRNKvAGGKMKKRK 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 |
3.56e-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: 437.90 E-value: 3.56e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 25 TFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTREL 104
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPILQALLENPQRFFALVLAPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 105 AFQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDF 184
Cdd:cd17954 81 AQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKGFSLKSLKFLVMDEADRLLNMDF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 52782792 185 ETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCA 227
Cdd:cd17954 161 EPEIDKILKVIPRERTTYLFSATMTTKVAKLQRASLKNPVKIE 203
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
24-446 |
6.63e-94 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 290.31 E-value: 6.63e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 24 KTFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFA----LVLT 99
Cdd:PRK11192 1 TTFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPALQHLLDFPRRKSGppriLILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 100 PTRELAFQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKgFNLRALKYLVMDEADRI 179
Cdd:PRK11192 81 PTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEEN-FDCRAVETLILDEADRM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 180 LNMDFETEVDKILKVIpRDRK-TFLFSATMT-KKVQKLQRAALKNPVKCAVSSKYQTVEKLQQ-YYIFIPSKFKDTYLVY 256
Cdd:PRK11192 160 LDMGFAQDIETIAAET-RWRKqTLLFSATLEgDAVQDFAERLLNDPVEVEAEPSRRERKKIHQwYYRADDLEHKTALLCH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 257 ILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVV 336
Cdd:PRK11192 239 LLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATDVAARGIDIDDVSHVI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 337 NFDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIEHLIGKKL-PGF-----PTQDDEVMMLTERVAEAQRFA 410
Cdd:PRK11192 319 NFDMPRSADTYLHRIGRTGRAGRKGTAISLVEAHDHLLLGKIERYIEEPLkARVidelrPKTKAPSEKKTGKPSKKVLAK 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 52782792 411 RMELREHGEKKKRSREDAGDNDdtegAIGVRNKVAG 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 |
6.17e-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: 279.49 E-value: 6.17e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 26 FKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELA 105
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSEDPYGIFALVLTPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 106 FQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKG--FNLRALKYLVMDEADRILNMD 183
Cdd:cd17955 81 YQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRSSDDttKVLSRVKFLVLDEADRLLTGS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 52782792 184 FETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCA 227
Cdd:cd17955 161 FEDDLATILSALPPKRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
40-386 |
2.77e-92 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 287.08 E-value: 2.77e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 40 DQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELAFQISEQFEALGSSI 119
Cdd:PRK11776 20 NELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKLDVKRFRVQALVLCPTRELADQVAKEIRRLARFI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 120 -GVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLEntKG-FNLRALKYLVMDEADRILNMDFETEVDKILKVIPR 197
Cdd:PRK11776 100 pNIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLR--KGtLDLDALNTLVLDEADRMLDMGFQDAIDAIIRQAPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 198 DRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTvEKLQQYYIFIPSKFKDTYLVYILNELAGNSFMIFCSTCNNTQ 277
Cdd:PRK11776 178 RRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDL-PAIEQRFYEVSPDERLPALQRLLLHHQPESCVVFCNTKKECQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 278 RTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARA 357
Cdd:PRK11776 257 EVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVATDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRA 336
|
330 340
....*....|....*....|....*....
gi 52782792 358 GRSGKAITFVTQYDVELFQRIEHLIGKKL 386
Cdd:PRK11776 337 GSKGLALSLVAPEEMQRANAIEDYLGRKL 365
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
25-368 |
1.62e-91 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 287.83 E-value: 1.62e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 25 TFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPIL-----NALLETPQRLFALVLT 99
Cdd:PTZ00110 131 SFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIvhinaQPLLRYGDGPIVLVLA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 100 PTRELAFQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKGfNLRALKYLVMDEADRI 179
Cdd:PTZ00110 211 PTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLESNVT-NLRRVTYLVLDEADRM 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 180 LNMDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKN-PVKCAVSS-KYQTVEKLQQYYIFIPSKFKDTYLVYI 257
Cdd:PTZ00110 290 LDMGFEPQIRKIVSQIRPDRQTLMWSATWPKEVQSLARDLCKEePVHVNVGSlDLTACHNIKQEVFVVEEHEKRGKLKML 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 258 LNEL--AGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVV 335
Cdd:PTZ00110 370 LQRImrDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYV 449
|
330 340 350
....*....|....*....|....*....|...
gi 52782792 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 |
1.31e-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: 273.16 E-value: 1.31e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 35 LCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLF----ALVLTPTRELAFQISE 110
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPKKKGrgpqALVLAPTRELAMQIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 111 QFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKgFNLRALKYLVMDEADRILNMDFETEVDK 190
Cdd:cd00268 81 VARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGK-LDLSNVKYLVLDEADRMLDMGFEEDVEK 159
|
170 180 190
....*....|....*....|....*....|....*
gi 52782792 191 ILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVK 225
Cdd:cd00268 160 ILSALPKDRQTLLFSATLPEEVKELAKKFLKNPVR 194
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
20-387 |
7.25e-86 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 275.19 E-value: 7.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 20 EEETkTFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNAL---LETPQrlfAL 96
Cdd:PRK11634 3 EFET-TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNLdpeLKAPQ---IL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 97 VLTPTRELAFQISEQFEALGSSI-GVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKgFNLRALKYLVMDE 175
Cdd:PRK11634 79 VLAPTRELAVQVAEAMTDFSKHMrGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGT-LDLSKLSGLVLDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 176 ADRILNMDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYIFIPSKFKDTYLV 255
Cdd:PRK11634 158 ADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 256 YILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVV 335
Cdd:PRK11634 238 RFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 52782792 336 VNFDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIEHLIGKKLP 387
Cdd:PRK11634 318 VNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIP 369
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
25-455 |
3.77e-77 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 251.02 E-value: 3.77e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 25 TFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALL-------ETPQRLFALV 97
Cdd:PRK04537 10 TFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLsrpaladRKPEDPRALI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 98 LTPTRELAFQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKGFNLRALKYLVMDEAD 177
Cdd:PRK04537 90 LAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHKVVSLHACEICVLDEAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 178 RILNMDFETEVDKILKVIPR--DRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYIFIPSKFKDTYLV 255
Cdd:PRK04537 170 RMFDLGFIKDIRFLLRRMPErgTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAARVRQRIYFPADEEKQTLLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 256 YILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVV 335
Cdd:PRK04537 250 GLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDVAARGLHIDGVKYV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 336 VNFDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIEHLIGKKLPGFPtqddevmMLTERVAEAQRFARMELR 415
Cdd:PRK04537 330 YNYDLPFDAEDYVHRIGRTARLGEEGDAISFACERYAMSLPDIEAYIEQKIPVEP-------VTAELLTPLPRPPRVPVE 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 52782792 416 EHGEKkkrsredaGDNDDTEGAIG--VRNKVAGGKMKKRKGR 455
Cdd:PRK04537 403 GEEAD--------DEAGDSVGTIFreAREQRAAEEQRRGGGR 436
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
25-387 |
4.21e-77 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 247.80 E-value: 4.21e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 25 TFKDLGVT-DVLCEACDQlGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQR------LFALV 97
Cdd:PRK10590 2 SFDSLGLSpDILRAVAEQ-GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHakgrrpVRALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 98 LTPTRELAFQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDhLENTKGFNLRALKYLVMDEAD 177
Cdd:PRK10590 81 LTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLD-LEHQNAVKLDQVEILVLDEAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 178 RILNMDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYIFIPSKFKDTYLVYI 257
Cdd:PRK10590 160 RMLDMGFIHDIRRVLAKLPAKRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVTQHVHFVDKKRKRELLSQM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 258 LNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVN 337
Cdd:PRK10590 240 IGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVVN 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 52782792 338 FDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIEHLIGKKLP 387
Cdd:PRK10590 320 YELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLKKEIP 369
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
35-225 |
1.18e-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: 1.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 35 LCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLF---ALVLTPTRELAFQISEQ 111
Cdd:cd17947 1 LLRALSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERLLYRPKKKAatrVLVLVPTRELAMQCFSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 112 FEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDFETEVDKI 191
Cdd:cd17947 81 LQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPSFDLDSIEILVLDEADRMLEEGFADELKEI 160
|
170 180 190
....*....|....*....|....*....|....
gi 52782792 192 LKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVK 225
Cdd:cd17947 161 LRLCPRTRQTMLFSATMTDEVKDLAKLSLNKPVR 194
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
17-386 |
8.85e-75 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 242.13 E-value: 8.85e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 17 IVEEEETKT-FKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETP---QR 92
Cdd:PRK01297 79 VVEPQEGKTrFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPppkER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 93 LF----ALVLTPTRELAFQISEQFEALGSSIGVQSAVIVGGIDSMSQSLAL-AKKPHIIIATPGRLIDHLENtKGFNLRA 167
Cdd:PRK01297 159 YMgeprALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLeARFCDILVATPGRLLDFNQR-GEVHLDM 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 168 LKYLVMDEADRILNMDFETEVDKILKVIPR--DRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYIFI 245
Cdd:PRK01297 238 VEVMVLDEADRMLDMGFIPQVRQIIRQTPRkeERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYAV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 246 PSKFKDTYLVYILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASR 325
Cdd:PRK01297 318 AGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGR 397
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52782792 326 GLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIEHLIGKKL 386
Cdd:PRK01297 398 GIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISFAGEDDAFQLPEIEELLGRKI 458
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
1-379 |
5.52e-66 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 217.00 E-value: 5.52e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 1 MAAPEE-HDSPTEASQPIVE---EEETKTFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTG 76
Cdd:PTZ00424 1 MATSEQkNQSEQVASTGTIEsnyDEIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 77 AF---ALPILNALLETPQrlfALVLTPTRELAFQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRL 153
Cdd:PTZ00424 81 TFviaALQLIDYDLNACQ---ALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 154 IDHLENtKGFNLRALKYLVMDEADRILNMDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQ 233
Cdd:PTZ00424 158 YDMIDK-RHLRVDDLKLFILDEADEMLSRGFKGQIYDVFKKLPPDVQVALFSATMPNEILELTTKFMRDPKRILVKKDEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 234 TVEKLQQYYIFIPS-KFKDTYLVYILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAK 312
Cdd:PTZ00424 237 TLEGIRQFYVAVEKeEWKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSG 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52782792 313 ARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIE 379
Cdd:PTZ00424 317 STRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDIEQLKEIE 383
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
35-224 |
2.17e-64 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350703 [Multi-domain] Cd Length: 220 Bit Score: 206.79 E-value: 2.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 35 LCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRL--------FALVLTPTRELAF 106
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPPLDeetkddgpYALILAPTRELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 107 QISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENtKGFNLRALKYLVMDEADRILNMDFET 186
Cdd:cd17945 81 QIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLER-RLLVLNQCTYVVLDEADRMIDMGFEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 52782792 187 EVDKILKVIP--------------------RDRKTFLFSATMTKKVQKLQRAALKNPV 224
Cdd:cd17945 160 QVTKILDAMPvsnkkpdteeaeklaasgkhRYRQTMMFTATMPPAVEKIAKGYLRRPV 217
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
23-387 |
4.72e-64 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 212.52 E-value: 4.72e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 23 TKTFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQ---------Rl 93
Cdd:PRK04837 7 EQKFSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLSHPApedrkvnqpR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 94 fALVLTPTRELAFQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENtKGFNLRALKYLVM 173
Cdd:PRK04837 86 -ALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQ-NHINLGAIQVVVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 174 DEADRILNMDFETEVDKILKVIP--RDRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQyYIFIPSK-FK 250
Cdd:PRK04837 164 DEADRMFDLGFIKDIRWLFRRMPpaNQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKE-ELFYPSNeEK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 251 DTYLVYILNELAGNSFMIFCST---CNNT--------QRTALLLrnlgftaiplhGQMSQSKRLGSLNKFKAKARSILLA 319
Cdd:PRK04837 243 MRLLQTLIEEEWPDRAIIFANTkhrCEEIwghlaadgHRVGLLT-----------GDVAQKKRLRILEEFTRGDLDILVA 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52782792 320 TDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITFV-TQYDVELfQRIEHLIGKKLP 387
Cdd:PRK04837 312 TDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLAcEEYALNL-PAIETYIGHSIP 379
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
25-222 |
2.53e-63 |
|
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: 204.26 E-value: 2.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 25 TFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRL----------F 94
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSvgrgrrkaypS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 95 ALVLTPTRELAFQISEQ---FeALGSsiGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKgFNLRALKYL 171
Cdd:cd17967 81 ALILAPTRELAIQIYEEarkF-SYRS--GVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGR-ISLSSIKFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 52782792 172 VMDEADRILNMDFETEVDKILK----VIPRDRKTFLFSATMTKKVQKLQRAALKN 222
Cdd:cd17967 157 VLDEADRMLDMGFEPQIRKIVEhpdmPPKGERQTLMFSATFPREIQRLAADFLKN 211
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
33-224 |
1.77e-61 |
|
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: 198.96 E-value: 1.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 33 DVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLE------TPQRLFALVLTPTRELAF 106
Cdd:cd17961 3 PRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKakaesgEEQGTRALILVPTRELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 107 QISEQFEALGSSIG--VQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDF 184
Cdd:cd17961 83 QVSKVLEQLTAYCRkdVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLSTLKYLVIDEADLVLSYGY 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 52782792 185 ETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPV 224
Cdd:cd17961 163 EEDLKSLLSYLPKNYQTFLMSATLSEDVEALKKLVLHNPA 202
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
48-215 |
1.45e-60 |
|
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: 194.77 E-value: 1.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 48 TKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELAFQISEQFEALGSSIGVQSAVIV 127
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNGPQALVLAPTRELAEQIYEELKKLGKGLGLKVASLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 128 GGiDSMSQSLALAKKPHIIIATPGRLIDHLENTKgfNLRALKYLVMDEADRILNMDFETEVDKILKVIPRDRKTFLFSAT 207
Cdd:pfam00270 81 GG-DSRKEQLEKLKGPDILVGTPGRLLDLLQERK--LLKNLKLLVLDEAHRLLDMGFGPDLEEILRRLPKKRQILLLSAT 157
|
....*...
gi 52782792 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 |
2.65e-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: 2.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 41 QLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPIL-----NALLETPQRLFALVLTPTRELAFQISEQFEAL 115
Cdd:cd17966 7 RQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPAIvhinaQPPLERGDGPIVLVLAPTRELAQQIQQEANKF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 116 GSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKGfNLRALKYLVMDEADRILNMDFETEVDKILKVI 195
Cdd:cd17966 87 GGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKT-NLRRVTYLVLDEADRMLDMGFEPQIRKIVDQI 165
|
170 180 190
....*....|....*....|....*....|
gi 52782792 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 |
5.74e-59 |
|
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: 189.64 E-value: 5.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 238 LQQYYIFIPSKFKDTYL-VYILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSI 316
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLlLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 52782792 317 LLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITFV 367
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
25-226 |
4.82e-58 |
|
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: 189.82 E-value: 4.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 25 TFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQR--LFALVLTPTR 102
Cdd:cd17959 2 GFQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLKAHSPTvgARALILSPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 103 ELAFQISEQFEALGSSIGVQSAVIVGGiDSM-SQSLALAKKPHIIIATPGRLIDHLENTkGFNLRALKYLVMDEADRILN 181
Cdd:cd17959 82 ELALQTLKVTKELGKFTDLRTALLVGG-DSLeEQFEALASNPDIIIATPGRLLHLLVEM-NLKLSSVEYVVFDEADRLFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 52782792 182 MDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKC 226
Cdd:cd17959 160 MGFAEQLHEILSRLPENRQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
43-224 |
5.32e-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: 189.42 E-value: 5.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 43 GWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLE---TPQR-LFALVLTPTRELAFQISEQFEALGSS 118
Cdd:cd17941 9 GFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRerwTPEDgLGALIISPTRELAMQIFEVLRKVGKY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 119 IGVQSAVIVGGIDSMSQSLALAKKpHIIIATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDFETEVDKILKVIPRD 198
Cdd:cd17941 89 HSFSAGLIIGGKDVKEEKERINRM-NILVCTPGRLLQHMDETPGFDTSNLQMLVLDEADRILDMGFKETLDAIVENLPKS 167
|
170 180
....*....|....*....|....*.
gi 52782792 199 RKTFLFSATMTKKVQKLQRAALKNPV 224
Cdd:cd17941 168 RQTLLFSATQTKSVKDLARLSLKNPE 193
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
42-239 |
2.93e-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: 186.29 E-value: 2.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 42 LGWTKPTKIQIEAIPLAL-QGRDIIGLAETGSGKTGAFALPILNALLE--------TPQR-LFALVLTPTRELAFQISEQ 111
Cdd:cd17946 8 LGFSEPTPIQALALPAAIrDGKDVIGAAETGSGKTLAFGIPILERLLSqkssngvgGKQKpLRALILTPTRELAVQVKDH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 112 FEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKGF--NLRALKYLVMDEADRIL-NMDFEtEV 188
Cdd:cd17946 88 LKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHlaNLKSLRFLVLDEADRMLeKGHFA-EL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 52782792 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 |
4.05e-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: 182.17 E-value: 4.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 38 ACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALP---ILNALLETPQR-LFALVLTPTRELAFQISEQFE 113
Cdd:cd17942 4 AIEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPaieLLYKLKFKPRNgTGVIIISPTRELALQIYGVAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 114 ALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDFETEVDKILK 193
Cdd:cd17942 84 ELLKYHSQTFGIVIGGANRKAEAEKLGKGVNILVATPGRLLDHLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQIIK 163
|
170 180 190
....*....|....*....|....*....|
gi 52782792 194 VIPRDRKTFLFSATMTKKVQKLQRAALKNP 223
Cdd:cd17942 164 LLPKRRQTMLFSATQTRKVEDLARISLKKK 193
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
25-376 |
6.87e-55 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 190.77 E-value: 6.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 25 TFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNAL-------LETPQRLFALV 97
Cdd:PLN00206 122 SFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCctirsghPSEQRNPLAMV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 98 LTPTRELAFQISEQFEALGSSIGVQSAVIVGGiDSMSQSLALAKKP-HIIIATPGRLIDHLeNTKGFNLRALKYLVMDEA 176
Cdd:PLN00206 202 LTPTRELCVQVEDQAKVLGKGLPFKTALVVGG-DAMPQQLYRIQQGvELIVGTPGRLIDLL-SKHDIELDNVSVLVLDEV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 177 DRILNMDFETEVDKILKVIPRDrKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYIFIPSKFKDTYLVY 256
Cdd:PLN00206 280 DCMLERGFRDQVMQIFQALSQP-QVLLFSATVSPEVEKFASSLAKDIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFD 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 257 ILneLAGNSFMIFCSTCNNTQRTALLLRN-----LGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPH 331
Cdd:PLN00206 359 IL--KSKQHFKPPAVVFVSSRLGADLLANaitvvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLR 436
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 52782792 332 VDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQ 376
Cdd:PLN00206 437 VRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFP 481
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
42-224 |
1.44e-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: 1.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 42 LGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRL------FALVLTPTRELAFQISEQFEAL 115
Cdd:cd17949 9 MGIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPRVdrsdgtLALVLVPTRELALQIYEVLEKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 116 GS-SIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDFETEVDKILKV 194
Cdd:cd17949 89 LKpFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQSFDVSNLRWLVLDEADRLLDMGFEKDITKILEL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 52782792 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 |
2.52e-53 |
|
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: 178.34 E-value: 2.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 24 KTFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETP-----QRLFALVL 98
Cdd:cd17953 12 QKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQRpvkpgEGPIGLIM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 99 TPTRELAFQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHL--ENTKGFNLRALKYLVMDEA 176
Cdd:cd17953 92 APTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILtaNNGRVTNLRRVTYVVLDEA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 52782792 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 |
8.13e-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: 176.38 E-value: 8.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 46 KPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRL--------FALVLTPTRELA---FQISEQF-E 113
Cdd:cd17951 12 KPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLpfikgegpYGLIVCPSRELArqtHEVIEYYcK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 114 AL--GSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLeNTKGFNLRALKYLVMDEADRILNMDFETEVDKI 191
Cdd:cd17951 92 ALqeGGYPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDML-NKKKINLDICRYLCLDEADRMIDMGFEEDIRTI 170
|
170 180 190
....*....|....*....|....*....|...
gi 52782792 192 LKVIPRDRKTFLFSATMTKKVQKLQRAALKNPV 224
Cdd:cd17951 171 FSYFKGQRQTLLFSATMPKKIQNFAKSALVKPV 203
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
35-225 |
1.71e-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: 1.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 35 LCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRL-----FALVLTPTRELAFQIS 109
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQRELEkgegpIAVIVAPTRELAQQIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 110 EQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLEnTKGFNLRALKYLVMDEADRILNMDFETEVD 189
Cdd:cd17952 81 LEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVK-KKATNLQRVTYLVLDEADRMFDMGFEYQVR 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 52782792 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 |
4.31e-52 |
|
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350718 [Multi-domain] Cd Length: 202 Bit Score: 174.30 E-value: 4.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 37 EACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALL-----ETPQRLFALVLTPTRELAFQISEQ 111
Cdd:cd17960 3 DVVAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLkrkanLKKGQVGALIISPTRELATQIYEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 112 FEALGSSIG--VQSAVIVGGIDSMSQSLAL-AKKPHIIIATPGRLIDHLENTKG-FNLRALKYLVMDEADRILNMDFETE 187
Cdd:cd17960 83 LQSFLEHHLpkLKCQLLIGGTNVEEDVKKFkRNGPNILVGTPGRLEELLSRKADkVKVKSLEVLVLDEADRLLDLGFEAD 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 52782792 188 VDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVK 225
Cdd:cd17960 163 LNRILSKLPKQRRTGLFSATQTDAVEELIKAGLRNPVR 200
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
31-221 |
1.01e-51 |
|
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: 173.54 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 31 VTDVLCEACDQLGWTKPTKIQIEAIPLALQ-GRDIIGLAETGSGKTGAFALPILNALLETPQRL-----FALVLTPTREL 104
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILStGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGrrsgvSALIISPTREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 105 AFQISEQFEAL---GSSIGVQSAVivGGIDSMSQSLALAK-KPHIIIATPGRLIDHLENTKGFN-LRALKYLVMDEADRI 179
Cdd:cd17964 81 ALQIAAEAKKLlqgLRKLRVQSAV--GGTSRRAELNRLRRgRPDILVATPGRLIDHLENPGVAKaFTDLDYLVLDEADRL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 52782792 180 LNMDFETEVDKILKVIP----RDRKTFLFSATMTKKVQKLQRAALK 221
Cdd:cd17964 159 LDMGFRPDLEQILRHLPeknaDPRQTLLFSATVPDEVQQIARLTLK 204
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
41-241 |
3.01e-51 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 171.91 E-value: 3.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 41 QLGWTKPTKIQIEAIPLALQG-RDIIGLAETGSGKTGAFALPILNALLETPQRlFALVLTPTRELAFQISEQFEALGSSI 119
Cdd:smart00487 3 KFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGG-RVLVLVPTRELAEQWAEELKKLGPSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 120 GVQSAVIVGGIDSMSQSLALAK-KPHIIIATPGRLIDHLENtKGFNLRALKYLVMDEADRILNMDFETEVDKILKVIPRD 198
Cdd:smart00487 82 GLKVVGLYGGDSKREQLRKLESgKTDILVTTPGRLLDLLEN-DKLSLSNVDLVILDEAHRLLDGGFGDQLEKLLKLLPKN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 52782792 199 RKTFLFSATMTKKVQKLQRAALKNPVKcaVSSKYQTVEKLQQY 241
Cdd:smart00487 161 VQLLLLSATPPEEIENLLELFLNDPVF--IDVGFTPLEPIEQF 201
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
43-228 |
1.63e-50 |
|
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: 170.08 E-value: 1.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 43 GWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQR--LFALVLTPTRELAFQISEQFEALGSSIG 120
Cdd:cd17957 9 GYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKkgLRALILAPTRELASQIYRELLKLSKGTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 121 VQSAVIVGGI-DSMSQSLALAKKPHIIIATPGRLIDHLENTKgFNLRALKYLVMDEADRILNMDFETEVDKILKVI--PR 197
Cdd:cd17957 89 LRIVLLSKSLeAKAKDGPKSITKYDILVSTPLRLVFLLKQGP-IDLSSVEYLVLDEADKLFEPGFREQTDEILAACtnPN 167
|
170 180 190
....*....|....*....|....*....|.
gi 52782792 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 |
1.59e-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: 169.76 E-value: 1.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 25 TFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLET---------PQRLFA 95
Cdd:cd18052 44 TFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPVLTGMMKEgltassfseVQEPQA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 96 LVLTPTRELAFQIseQFEALGSSIG--VQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKgFNLRALKYLVM 173
Cdd:cd18052 124 LIVAPTRELANQI--FLEARKFSYGtcIRPVVVYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGK-ISLSKLKYLIL 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 52782792 174 DEADRILNMDFETEVDKILKV--IPR--DRKTFLFSATMTKKVQKLQRAALK 221
Cdd:cd18052 201 DEADRMLDMGFGPEIRKLVSEpgMPSkeDRQTLMFSATFPEEIQRLAAEFLK 252
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
26-225 |
1.65e-49 |
|
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or p54) participates in mRNA regulation mediated by miRNA-mediated silencing. It also plays a role in global and transcript-specific messenger RNA (mRNA) storage, translational repression, and decay. It is a member of the DEAD-box helicase family, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350698 [Multi-domain] Cd Length: 201 Bit Score: 167.47 E-value: 1.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 26 FKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELA 105
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPKKDVIQALILVPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 106 FQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDhLENTKGFNLRALKYLVMDEADRILNMDFE 185
Cdd:cd17940 81 LQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILD-LAKKGVADLSHCKTLVLDEADKLLSQDFQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 52782792 186 TEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVK 225
Cdd:cd17940 160 PIIEKILNFLPKERQILLFSATFPLTVKNFMDRHMHNPYE 199
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
8-228 |
2.15e-47 |
|
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: 163.67 E-value: 2.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 8 DSPTEASQPIVEEEeTKTFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALL 87
Cdd:cd18051 6 DIPVEATGENCPPH-IETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPILSQIY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 88 ET----------------PQRLFALVLTPTRELAFQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPG 151
Cdd:cd18051 85 EQgpgeslpsesgyygrrKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLVATPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 152 RLIDHLENTKgFNLRALKYLVMDEADRILNMDFETEVDKILK--VIPR--DRKTFLFSATMTKKVQKLQRAALKNPVKCA 227
Cdd:cd18051 165 RLVDMLERGK-IGLDYCKYLVLDEADRMLDMGFEPQIRRIVEqdTMPPtgERQTLMFSATFPKEIQMLARDFLDNYIFLA 243
|
.
gi 52782792 228 V 228
Cdd:cd18051 244 V 244
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
37-224 |
9.87e-47 |
|
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: 159.94 E-value: 9.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 37 EACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETP----QRL--FALVLTPTRELAFQISE 110
Cdd:cd17958 3 KEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQPipreQRNgpGVLVLTPTRELALQIEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 111 QFEALgSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDhLENTKGFNLRALKYLVMDEADRILNMDFETEVDK 190
Cdd:cd17958 83 ECSKY-SYKGLKSVCVYGGGNRNEQIEDLSKGVDIIIATPGRLND-LQMNNVINLKSITYLVLDEADRMLDMGFEPQIRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 52782792 191 ILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPV 224
Cdd:cd17958 161 ILLDIRPDRQTIMTSATWPDGVRRLAQSYLKDPM 194
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
35-223 |
1.66e-46 |
|
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: 160.49 E-value: 1.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 35 LCEACDQLGWTKPTKIQIEAIPLALQG---------RDIIGLAETGSGKTGAFALPILNALLETP-QRLFALVLTPTREL 104
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSKRVvPRLRALIVVPTKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 105 AFQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPH--------IIIATPGRLIDHLENTKGFNLRALKYLVMDEA 176
Cdd:cd17956 81 VQQVYKVFESLCKGTGLKVVSLSGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNSTPGFTLKHLRFLVIDEA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52782792 177 DRILNMDFETEVDKILKVIPRDRKT--------------------FLFSATMTKKVQKLQRAALKNP 223
Cdd:cd17956 161 DRLLNQSFQDWLETVMKALGRPTAPdlgsfgdanllersvrplqkLLFSATLTRDPEKLSSLKLHRP 227
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
26-224 |
3.66e-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: 158.64 E-value: 3.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 26 FKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILnalletpQRLFALVLTPTRELA 105
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-------QIVVALILEPSRELA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 106 FQISEQFEALGSSI---GVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKgFNLRALKYLVMDEADRILNM 182
Cdd:cd17938 74 EQTYNCIENFKKYLdnpKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGK-LDLSSVRFFVLDEADRLLSQ 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 52782792 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 |
8.48e-45 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350697 [Multi-domain] Cd Length: 199 Bit Score: 155.17 E-value: 8.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 43 GWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELAFQISEQFEALGSSIGVQ 122
Cdd:cd17939 16 GFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRETQALVLAPTRELAQQIQKVVKALGDYMGVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 123 SAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLeNTKGFNLRALKYLVMDEADRILNMDFETEVDKILKVIPRDRKTF 202
Cdd:cd17939 96 VHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDML-QRRSLRTDKIKMFVLDEADEMLSRGFKDQIYDIFQFLPPETQVV 174
|
170 180
....*....|....*....|...
gi 52782792 203 LFSATMTKKVQKLQRAALKNPVK 225
Cdd:cd17939 175 LFSATMPHEVLEVTKKFMRDPVR 197
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
43-225 |
1.63e-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: 154.24 E-value: 1.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 43 GWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELAFQISEQFEALGSSI-GV 121
Cdd:cd17962 9 GYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNPSALILTPTRELAVQIEDQAKELMKGLpPM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 122 QSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLeNTKGFNLRALKYLVMDEADRILNMDFETEVDKILKVIPRDRKT 201
Cdd:cd17962 89 KTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDIL-KQSSVELDNIKIVVVDEADTMLKMGFQQQVLDILENISHDHQT 167
|
170 180
....*....|....*....|....
gi 52782792 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 |
1.41e-42 |
|
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: 151.70 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 31 VTDVLCeacdQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPIL-----NALLETPQRLFALVLTPTRELA 105
Cdd:cd18050 73 VMDVLL----DQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIvhinhQPYLERGDGPICLVLAPTRELA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 106 FQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKGfNLRALKYLVMDEADRILNMDFE 185
Cdd:cd18050 149 QQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRMLDMGFE 227
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 52782792 186 TEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCAV 228
Cdd:cd18050 228 PQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
44-230 |
3.21e-42 |
|
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: 149.39 E-value: 3.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 44 WTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPIL-----NALLETPQRLFALVLTPTRELAFQISEQFEALGSS 118
Cdd:cd18049 44 FTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIvhinhQPFLERGDGPICLVLAPTRELAQQVQQVAAEYGRA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 119 IGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKGfNLRALKYLVMDEADRILNMDFETEVDKILKVIPRD 198
Cdd:cd18049 124 CRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLEAGKT-NLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIRPD 202
|
170 180 190
....*....|....*....|....*....|..
gi 52782792 199 RKTFLFSATMTKKVQKLQRAALKNPVKCAVSS 230
Cdd:cd18049 203 RQTLMWSATWPKEVRQLAEDFLKDYIHINIGA 234
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
26-224 |
2.75e-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: 143.25 E-value: 2.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 26 FKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELA 105
Cdd:cd17950 4 FRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGQVSVLVICHTRELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 106 FQISEQFEALGSSI-GVQSAVIVGGIDSMSQSLALAKK-PHIIIATPGRLIDHLENtKGFNLRALKYLVMDEADRIL-NM 182
Cdd:cd17950 84 FQISNEYERFSKYMpNVKTAVFFGGVPIKKDIEVLKNKcPHIVVGTPGRILALVRE-KKLKLSHVKHFVLDECDKMLeQL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 52782792 183 DFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPV 224
Cdd:cd17950 163 DMRRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQDPL 204
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
42-225 |
4.13e-36 |
|
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: 131.93 E-value: 4.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 42 LGWTKPTKIQIEAIPLALQG--RDIIGLAETGSGKTGAFALPIL---NALLETPQrlfALVLTPTRELAFQISEQFEALG 116
Cdd:cd17963 12 MGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLsrvDPTLKSPQ---ALCLAPTRELARQIGEVVEKMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 117 SSIGVQSAVIVGGIDSMSQSLALAkkpHIIIATPGRLIDHLEnTKGFNLRALKYLVMDEADRILNMD-FETEVDKILKVI 195
Cdd:cd17963 89 KFTGVKVALAVPGNDVPRGKKITA---QIVIGTPGTVLDWLK-KRQLDLKKIKILVLDEADVMLDTQgHGDQSIRIKRML 164
|
170 180 190
....*....|....*....|....*....|
gi 52782792 196 PRDRKTFLFSATMTKKVQKLQRAALKNPVK 225
Cdd:cd17963 165 PRNCQILLFSATFPDSVRKFAEKIAPNANT 194
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
43-207 |
4.31e-36 |
|
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: 131.62 E-value: 4.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 43 GWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELAFQISEQFEALGSSI-GV 121
Cdd:cd17943 9 GFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESLDLERRHPQVLILAPTREIAVQIHDVFKKIGKKLeGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 122 QSAVIVGGIDsMSQSLALAKKPHIIIATPGRlIDHLENTKGFNLRALKYLVMDEADRILNMDFETEVDKILKVIPRDRKT 201
Cdd:cd17943 89 KCEVFIGGTP-VKEDKKKLKGCHIAVGTPGR-IKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNWIFSSLPKNKQV 166
|
....*.
gi 52782792 202 FLFSAT 207
Cdd:cd17943 167 IAFSAT 172
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
26-225 |
1.20e-34 |
|
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: 127.95 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 26 FKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNAL---LETPQrlfALVLTPTR 102
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIdtsLKATQ---ALVLAPTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 103 ELAFQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLeNTKGFNLRALKYLVMDEADRILNM 182
Cdd:cd18046 78 ELAQQIQKVVMALGDYMGIKCHACIGGTSVRDDAQKLQAGPHIVVGTPGRVFDMI-NRRYLRTDYIKMFVLDEADEMLSR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 52782792 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 |
6.87e-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: 6.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 250 KDTYLVYILNELAGNSFMIFCSTCNNTQrTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDI 329
Cdd:pfam00271 2 KLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDL 80
|
90 100
....*....|....*....|....*....
gi 52782792 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 |
7.36e-31 |
|
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: 117.95 E-value: 7.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 26 FKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELA 105
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILSPTRELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 106 FQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENtKGFNLRALKYLVMDEADRILNMDFE 185
Cdd:cd18045 81 VQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRR-RSLRTRHIKMLVLDEADEMLNKGFK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 52782792 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 |
3.01e-30 |
|
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: 117.08 E-value: 3.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 35 LCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALL---ETPQRLF----ALVLTPTRELAFQ 107
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLrykLLAEGPFnaprGLVITPSRELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 108 ISEQFEALGSSIGVQSAVIVGGidsmsQSLALAKKPH-----IIIATPGrLIDHLENTKGFNLRALKYLVMDEADRILNM 182
Cdd:cd17948 81 IGSVAQSLTEGLGLKVKVITGG-----RTKRQIRNPHfeevdILVATPG-ALSKLLTSRIYSLEQLRHLVLDEADTLLDD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 52782792 183 DFETEVDKILK-----------VIPRDRKT--FLFSATMTKKVQKL 215
Cdd:cd17948 155 SFNEKLSHFLRrfplasrrsenTDGLDPGTqlVLVSATMPSGVGEV 200
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
277-358 |
8.10e-27 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 102.68 E-value: 8.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 277 QRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTAR 356
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 52782792 357 AG 358
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
50-221 |
1.75e-26 |
|
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: 106.09 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 50 IQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLF------ALVLTPTRELAFQISEQFEALGSSIGVqs 123
Cdd:cd17944 16 IQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKrgrapkVLVLAPTRELANQVTKDFKDITRKLSV-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 124 AVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKgFNLRALKYLVMDEADRILNMDFETEVDKILKVI----PRDR 199
Cdd:cd17944 94 ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGR-LDLTKLKHVVLDEVDQMLDMGFAEQVEEILSVSykkdSEDN 172
|
170 180
....*....|....*....|...
gi 52782792 200 -KTFLFSATMTKKVQKLQRAALK 221
Cdd:cd17944 173 pQTLLFSATCPDWVYNVAKKYMK 195
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
24-223 |
4.61e-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: 91.62 E-value: 4.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 24 KTFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQG--RDIIGLAETGSGKTGAFALPIL---NALLETPQrlfALVL 98
Cdd:cd18048 18 KSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLsrvDALKLYPQ---CLCL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 99 TPTRELAFQISEQFEALGS-SIGVQSAVIVGGiDSMSQSLALAKKphIIIATPGRLIDHLENTKGFNLRALKYLVMDEAD 177
Cdd:cd18048 95 SPTFELALQTGKVVEEMGKfCVGIQVIYAIRG-NRPGKGTDIEAQ--IVIGTPGTVLDWCFKLRLIDVTNISVFVLDEAD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 52782792 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 |
2.74e-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: 85.93 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 24 KTFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQG--RDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPT 101
Cdd:cd18047 1 KSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 102 RELAFQISEQFEALGSSI-GVQSAVIVGGiDSMSQSLALakKPHIIIATPGRLIDHLENTKGFNLRALKYLVMDEAD-RI 179
Cdd:cd18047 81 YELALQTGKVIEQMGKFYpELKLAYAVRG-NKLERGQKI--SEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADvMI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 52782792 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 |
1.04e-18 |
|
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: 82.45 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 67 LAETGSGKTGAFALPILNALLEtpQRLFALVLTPTRELAFQISEQFEALgSSIGVQSAVIVGGIDSMSQSLALAKKPHII 146
Cdd:cd00046 7 TAPTGSGKTLAALLAALLLLLK--KGKKVLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGSSAEEREKNKLGDADII 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52782792 147 IATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDFETEVDK--ILKVIPRDRKTFLFSAT 207
Cdd:cd00046 84 IATPDMLLNLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDlaVRKAGLKNAQVILLSAT 146
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
41-217 |
1.86e-16 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 78.96 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 41 QLGWTKPTKIQIEAIPLALQ---------------GRDIIGLA-ETGSGKTGAFALPILNALLETPQRLF---------- 94
Cdd:cd17965 25 TDEEIKPSPIQTLAIKKLLKtlmrkvtkqtsneepKLEVFLLAaETGSGKTLAYLAPLLDYLKRQEQEPFeeaeeeyesa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 95 -------ALVLTPTRELAFQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALA--KKPHIIIATPGrLIDHLENTKGFNL 165
Cdd:cd17965 105 kdtgrprSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFGPSYQRLQLAfkGRIDILVTTPG-KLASLAKSRPKIL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 52782792 166 RALKYLVMDEADRILNMDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQR 217
Cdd:cd17965 184 SRVTHLVVDEADTLFDRSFLQDTTSIIKRAPKLKHLILCSATIPKEFDKTLR 235
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
51-437 |
2.22e-16 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 81.61 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 51 QIEAI-----PLALQGRDIIGLAETGSGKTGAFALpilnALLETPQRLFALVLTPTRELAFQISEQFEAL-------GSS 118
Cdd:COG1061 85 QQEALeallaALERGGGRGLVVAPTGTGKTVLALA----LAAELLRGKRVLVLVPRRELLEQWAEELRRFlgdplagGGK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 119 IGVQSAVIVGGIDSmsqslaLAKKPHIiiatpgrliDHLENTKGfnlralkYLVMDEADRILNMDFEtevdkilKVIPRD 198
Cdd:COG1061 161 KDSDAPITVATYQS------LARRAHL---------DELGDRFG-------LVIIDEAHHAGAPSYR-------RILEAF 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 199 RKTFL--FSAT------------------MTKKVQKLQRAALKNPVKC--------AVSSKYQTVEKLQQYYIFIPSKFK 250
Cdd:COG1061 212 PAAYRlgLTATpfrsdgreillflfdgivYEYSLKEAIEDGYLAPPEYygirvdltDERAEYDALSERLREALAADAERK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 251 DTYLVYILNELAGNSF-MIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDI 329
Cdd:COG1061 292 DKILRELLREHPDDRKtLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDV 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 330 PHVDVVVNFDiPTHSK-DYIHRVGRTARAGRSGKA---ITFVTQyDVELFQRIEHLIGKKLPGFPTQDDEVMMLTERVAE 405
Cdd:COG1061 372 PRLDVAILLR-PTGSPrEFIQRLGRGLRPAPGKEDalvYDFVGN-DVPVLEELAKDLRDLAGYRVEFLDEEESEELALLI 449
|
410 420 430
....*....|....*....|....*....|..
gi 52782792 406 AQRFARMELREHGEKKKRSREDAGDNDDTEGA 437
Cdd:COG1061 450 AVKPALEVKGELEEELLEELELLEDALLLVLA 481
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
35-176 |
1.03e-15 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 79.49 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 35 LCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPqRLFALVLTPTRELAF-Q---ISE 110
Cdd:COG1205 45 LRAALKKRGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLEDP-GATALYLYPTKALARdQlrrLRE 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52782792 111 QFEALGSSIGVqsAVIVGGIdSMSQSLALAKKPHIIIATP-----GrLIDHLENTKGFnLRALKYLVMDEA 176
Cdd:COG1205 124 LAEALGLGVRV--ATYDGDT-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 |
4.52e-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: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 51 QIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLfALVLTPTRELAFQISEQFEALGSSIGvqSAVIVGGI 130
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSR-ALYLYPTKALAQDQLRSLRELLEQLG--LGIRVATY 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 52782792 131 D---SMSQSLALAKK-PHIIIATPGRL---IDHLENTKGFNLRALKYLVMDEA 176
Cdd:cd17923 82 DgdtPREERRAIIRNpPRILLTNPDMLhyaLLPHHDRWARFLRNLRYVVLDEA 134
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
283-368 |
8.78e-12 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 67.45 E-value: 8.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 283 LRNLGFTAIPLHGQ--------MSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFD-IPTHSKdYIHRVGR 353
Cdd:COG1111 373 LSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEpVPSEIR-SIQRKGR 451
|
90
....*....|....*
gi 52782792 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 |
6.26e-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: 61.12 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 48 TKIQIEAIPLALQGRDIIGL-AETGSGKTGAFALPILNALLETPQRlfALVLTPTRELAFQISEQFEALGSSIGVQSAVI 126
Cdd:cd17921 3 NPIQREALRALYLSGDSVLVsAPTSSGKTLIAELAILRALATSGGK--AVYIAPTRALVNQKEADLRERFGPLGKNVGLL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 52782792 127 VGGIDSMSQSLAlakKPHIIIATPGRLIDHLENTKGFNLRALKYLVMDEA 176
Cdd:cd17921 81 TGDPSVNKLLLA---EADILVATPEKLDLLLRNGGERLIQDVRLVVVDEA 127
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
282-369 |
1.19e-09 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 60.66 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 282 LLRNLGFTAIPLHGQ--------MSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFD-IPTHSKdYIHRVG 352
Cdd:PRK13766 384 LLEKEGIKAVRFVGQaskdgdkgMSQKEQIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEIR-SIQRKG 462
|
90
....*....|....*..
gi 52782792 353 RTARaGRSGKAITFVTQ 369
Cdd:PRK13766 463 RTGR-QEEGRVVVLIAK 478
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
315-367 |
1.28e-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: 1.28e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 52782792 315 SILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAG-RSGKAITFV 367
Cdd:cd18785 24 EILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILFV 77
|
|
| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
61-175 |
1.62e-09 |
|
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: 56.82 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 61 GRDIIGLAETGSGKTGAFALPILNALL-ETPQRLFALVLTPTRELAFQISEQFEALGSSIGVQSAVIV--GGIDSMSQSL 137
Cdd:cd17922 1 GRNVLIAAPTGSGKTEAAFLPALSSLAdEPEKGVQVLYISPLKALINDQERRLEEPLDEIDLEIPVAVrhGDTSQSEKAK 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 52782792 138 ALAKKPHIIIATPGRLIDHLENTKGFN-LRALKYLVMDE 175
Cdd:cd17922 81 QLKNPPGILITTPESLELLLVNKKLRElFAGLRYVVVDE 119
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
296-357 |
3.84e-09 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 54.90 E-value: 3.84e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52782792 296 QMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRtARA 357
Cdd:cd18802 73 LMTQRKQKETLDKFRDGELNLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARA 133
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
51-433 |
1.01e-08 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 57.42 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 51 QIEAIPLALQGRDIIGLAETGSGKTGAFALP--ILNALletpqrlfALVLTPTRELAFQISEQFEALGSSigvqsAVIVG 128
Cdd:PRK11057 30 QQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPalVLDGL--------TLVVSPLISLMKDQVDQLLANGVA-----AACLN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 129 GIDSMSQSLALAKKPH-----IIIATPGRL-----IDHLENTKgfnlraLKYLVMDEADRI--LNMDFETEVDKILKVIP 196
Cdd:PRK11057 97 STQTREQQLEVMAGCRtgqikLLYIAPERLmmdnfLEHLAHWN------PALLAVDEAHCIsqWGHDFRPEYAALGQLRQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 197 R--DRKTFLFSATMTKKVQK--LQRAALKNPVkCAVSS------KYQTVEKlqqyyifipskFKDT-YLVYILNELAGNS 265
Cdd:PRK11057 171 RfpTLPFMALTATADDTTRQdiVRLLGLNDPL-IQISSfdrpniRYTLVEK-----------FKPLdQLMRYVQEQRGKS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 266 FMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSK 345
Cdd:PRK11057 239 GIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 346 DYIHRVGRTARAGRSGKAITFVTQYDVELFQRiehLIGKKLPGfPTQDDEVMMLTER--VAEAQRFARMELREH-GEkkk 422
Cdd:PRK11057 319 SYYQETGRAGRDGLPAEAMLFYDPADMAWLRR---CLEEKPAG-QQQDIERHKLNAMgaFAEAQTCRRLVLLNYfGE--- 391
|
410
....*....|.
gi 52782792 423 rSREDAGDNDD 433
Cdd:PRK11057 392 -GRQEPCGNCD 401
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
204-387 |
1.33e-08 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 56.69 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 204 FSATMTKKVQK--LQRAALKNPvKCAVSS------KYQTVEKLQQYyifipskfKDTYLVYILNELAGNSFMIFCSTCNN 275
Cdd:COG0514 172 LTATATPRVRAdiAEQLGLEDP-RVFVGSfdrpnlRLEVVPKPPDD--------KLAQLLDFLKEHPGGSGIVYCLSRKK 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 276 TQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATdVA-SRGLDIPHVDVVVNFDIPTHSKDYIHRVGRT 354
Cdd:COG0514 243 VEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRA 321
|
170 180 190
....*....|....*....|....*....|...
gi 52782792 355 ARAGRSGKAITFVTQYDVelfQRIEHLIGKKLP 387
Cdd:COG0514 322 GRDGLPAEALLLYGPEDV---AIQRFFIEQSPP 351
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
45-176 |
1.57e-08 |
|
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: 54.58 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 45 TKPTKIQIEAIPLALQgRDIIGLAETGSGKTGAFALPI-----LNALLETPQRlFALVLTPTRELAFQiseQFEALGSSI 119
Cdd:cd18034 1 FTPRSYQLELFEAALK-RNTIVVLPTGSGKTLIAVMLIkemgeLNRKEKNPKK-RAVFLVPTVPLVAQ---QAEAIRSHT 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52782792 120 GVQSAVIVGGIDSMSQS----LALAKKPHIIIATPGRLIDHLENTKgFNLRALKYLVMDEA 176
Cdd:cd18034 76 DLKVGEYSGEMGVDKWTkerwKEELEKYDVLVMTAQILLDALRHGF-LSLSDINLLIFDEC 135
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
297-364 |
2.36e-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: 52.74 E-value: 2.36e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52782792 297 MSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARaGRSGKAI 364
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVV 140
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
43-224 |
2.97e-08 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 53.69 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 43 GWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPilnALLETPqrlFALVLTPTRELafqISEQFEALgSSIGVQ 122
Cdd:cd17920 9 GYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLP---ALLLDG---VTLVVSPLISL---MQDQVDRL-QQLGIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 123 SAVIVGGIDSMSQSLALAK----KPHIIIATPGRL--------IDHLENTKGFNLralkyLVMDEADRILN--MDFETEV 188
Cdd:cd17920 79 AAALNSTLSPEEKREVLLRikngQYKLLYVTPERLlspdflelLQRLPERKRLAL-----IVVDEAHCVSQwgHDFRPDY 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 52782792 189 DKILKVIPRDRKT--FLFSATMTKKVQK--LQRAALKNPV 224
Cdd:cd17920 154 LRLGRLRRALPGVpiLALTATATPEVREdiLKRLGLRNPV 193
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
44-175 |
3.14e-08 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 55.88 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 44 WTKPTKIQIEAIPLALQGRDIIGLAETGSGKT-GAFaLPILNALLETP------QRLFALVLTPTRELAFQISEQFEALG 116
Cdd:COG1201 22 FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAF-LPALDELARRPrpgelpDGLRVLYISPLKALANDIERNLRAPL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52782792 117 SSIGVQSAVIVGGI-------D-SMSQSLALAKK-PHIIIATPgrlidhlE------NTKGF--NLRALKYLVMDE 175
Cdd:COG1201 101 EEIGEAAGLPLPEIrvgvrtgDtPASERQRQRRRpPHILITTP-------EslalllTSPDAreLLRGVRTVIVDE 169
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
51-207 |
1.43e-07 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 50.77 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 51 QIEAIPLALQ----GRDIIGLAeTGSGKTgAFALPILNALLETPqrlfALVLTPTRELAFQISEQFEALG--SSIGVQSA 124
Cdd:cd17926 5 QEEALEAWLAhknnRRGILVLP-TGSGKT-LTALALIAYLKELR----TLIVVPTDALLDQWKERFEDFLgdSSIGLIGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 125 VIVGGIDSMSqslalakkphIIIATPGRLIDHLENTKGFNLRALkYLVMDEADRILNMDFEtevdKILKvIPRDRKTFLF 204
Cdd:cd17926 79 GKKKDFDDAN----------VVVATYQSLSNLAEEEKDLFDQFG-LLIVDEAHHLPAKTFS----EILK-ELNAKYRLGL 142
|
...
gi 52782792 205 SAT 207
Cdd:cd17926 143 TAT 145
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
68-381 |
2.42e-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: 52.43 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 68 AETGSGKTGAfALPILNALLETPQRLFALVLTPTRELAFQISEQFEALGSSIGVQSAVIVG-GIDSMSQSLALAK----- 141
Cdd:cd09639 6 APTGYGKTEA-ALLWALHSLKSQKADRVIIALPTRATINAMYRRAKEAFGETGLYHSSILSsRIKEMGDSEEFEHlfply 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 142 ---------KPhIIIATPGRLIDHLENTKGFNLRAL-----KYLVMDEADRIL---NMDFETevdkILKVIPR-DRKTFL 203
Cdd:cd09639 85 ihsndtlflDP-ITVCTIDQVLKSVFGEFGHYEFTLasianSLLIFDEVHFYDeytLALILA----VLEVLKDnDVPILL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 204 FSATMTKKVQKLQRAALknPVKCAVSSKYQTVEKLQQYYIFIPSKFKDTYLVYILNEL-AGNSFMIFCSTCNNTQRTALL 282
Cdd:cd09639 160 MSATLPKFLKEYAEKIG--YVEENEPLDLKPNERAPFIKIESDKVGEISSLERLLEFIkKGGSVAIIVNTVDRAQEFYQQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 283 LRNLG--FTAIPLHGQMSQSKRLGS----LNKFKAKARSILLATDVASRGLDIpHVDVVVNFDIPTHSkdYIHRVGRTAR 356
Cdd:cd09639 238 LKEKGpeEEIMLIHSRFTEKDRAKKeaelLLEFKKSEKFVIVATQVIEASLDI-SVDVMITELAPIDS--LIQRLGRLHR 314
|
330 340 350
....*....|....*....|....*....|....*.
gi 52782792 357 AGRSGKAITFVTQ----------YDVELFQR-IEHL 381
Cdd:cd09639 315 YGEKNGEEVYIITdapdgkgqkpYPYDLVERtIELL 350
|
|
| DEXHc_HFM1 |
cd18023 |
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ... |
48-150 |
4.56e-07 |
|
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350781 [Multi-domain] Cd Length: 206 Bit Score: 50.43 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 48 TKIQIEAIPLALQG-RDIIGLAETGSGKTGAFALPILNALLETPQ----RLFALVLTPTRELAFQISEQFEALGSSIGVQ 122
Cdd:cd18023 3 NRIQSEVFPDLLYSdKNFVVSAPTGSGKTVLFELAILRLLKERNPlpwgNRKVVYIAPIKALCSEKYDDWKEKFGPLGLS 82
|
90 100
....*....|....*....|....*...
gi 52782792 123 SAVIVGgiDSMSQSLALAKKPHIIIATP 150
Cdd:cd18023 83 CAELTG--DTEMDDTFEIQDADIILTTP 108
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
51-175 |
5.80e-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: 49.64 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 51 QIEAI-PLALQGRDIIGLAETGSGKTGAFALPILNALLETPQrlfALVLTPTRELAFQISEQFEALgSSIGVQSAVIVGG 129
Cdd:cd18028 6 QAEAVrAGLLKGENLLISIPTASGKTLIAEMAMVNTLLEGGK---ALYLVPLRALASEKYEEFKKL-EEIGLKVGISTGD 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 52782792 130 IDSMSQSLAlakKPHIIIATPGRLiDHLENTKGFNLRALKYLVMDE 175
Cdd:cd18028 82 YDEDDEWLG---DYDIIVATYEKF-DSLLRHSPSWLRDVGVVVVDE 123
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
51-382 |
1.46e-06 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 51.05 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 51 QIEAIPLALQGRDIIGLAETGSGKTGAFALPilnALLETPqrlFALVLTPTRELafqISEQFEALGSSiGVQSAVIVGGI 130
Cdd:PLN03137 465 QREIINATMSGYDVFVLMPTGGGKSLTYQLP---ALICPG---ITLVISPLVSL---IQDQIMNLLQA-NIPAASLSAGM 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 131 DSMSQSLALAK------KPHIIIATPGR------LIDHLENTKGFNLraLKYLVMDEADRI--LNMDFETEVDK--ILKV 194
Cdd:PLN03137 535 EWAEQLEILQElsseysKYKLLYVTPEKvaksdsLLRHLENLNSRGL--LARFVIDEAHCVsqWGHDFRPDYQGlgILKQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 195 IPRDRKTFLFSATMTKKVQKLQRAALkNPVKCAVSSkyQTVEKLQQYYIFIPSKFKdtYLVYILNELAGNSF----MIFC 270
Cdd:PLN03137 613 KFPNIPVLALTATATASVKEDVVQAL-GLVNCVVFR--QSFNRPNLWYSVVPKTKK--CLEDIDKFIKENHFdecgIIYC 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 271 STCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHR 350
Cdd:PLN03137 688 LSRMDCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQE 767
|
330 340 350
....*....|....*....|....*....|..
gi 52782792 351 VGRtarAGRSGKAITFVTQYDVELFQRIEHLI 382
Cdd:PLN03137 768 CGR---AGRDGQRSSCVLYYSYSDYIRVKHMI 796
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
245-341 |
1.58e-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: 47.47 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 245 IPSKFKdtYLVYILNELAGNS--FMIFcstcnnTQRTALL------LRNLGFTAIPLHGQMSQSKRLGSLNKFKA--KAR 314
Cdd:cd18793 9 VSGKLE--ALLELLEELREPGekVLIF------SQFTDTLdileeaLRERGIKYLRLDGSTSSKERQKLVDRFNEdpDIR 80
|
90 100
....*....|....*....|....*..
gi 52782792 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 |
1.77e-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: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 267 MIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGS---LNKFKAKARSILLATDVASRGLDIPHVDVVVnFDIPTH 343
Cdd:cd18799 10 LIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDEaliLLFFGELKPPILVTVDLLTTGVDIPEVDNVV-FLRPTE 88
|
90
....*....|....
gi 52782792 344 SKD-YIHRVGRTAR 356
Cdd:cd18799 89 SRTlFLQMLGRGLR 102
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
48-175 |
5.57e-06 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 48.73 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 48 TKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALL------ETPQRLFALVLTPTRELA-----------FQISE 110
Cdd:PRK13767 34 TPPQRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELFrlgregELEDKVYCLYVSPLRALNndihrnleeplTEIRE 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52782792 111 QFEALGSSI-GVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRL-IdhLENTKGFN--LRALKYLVMDE 175
Cdd:PRK13767 114 IAKERGEELpEIRVAIRTGDTSSYEKQKMLKKPPHILITTPESLaI--LLNSPKFRekLRTVKWVIVDE 180
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
246-362 |
2.82e-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: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 246 PSKFKDTYLVYILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATdVA-S 324
Cdd:cd18794 13 KKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVAT-VAfG 91
|
90 100 110
....*....|....*....|....*....|....*...
gi 52782792 325 RGLDIPHVDVVVNFDIPTHSKDYIHRVGrtaRAGRSGK 362
Cdd:cd18794 92 MGIDKPDVRFVIHYSLPKSMESYYQESG---RAGRDGL 126
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
51-221 |
6.81e-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: 44.05 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 51 QIEAIPLALQGRDIIGLAETGSGKTGAFALPilnALLeTPQrlFALVLTPTRELafqISEQFEALgSSIGVQSAVIVGGI 130
Cdd:cd18016 22 QLEAINAALLGEDCFVLMPTGGGKSLCYQLP---ACV-SPG--VTVVISPLRSL---IVDQVQKL-TSLDIPATYLTGDK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 131 ---DSMSQSLALAKKPHII---------IATPGRLIDHLENTKGFNLraLKYLVMDEADRI--LNMDFETEVDKiLKVIp 196
Cdd:cd18016 92 tdaEATKIYLQLSKKDPIIkllyvtpekISASNRLISTLENLYERKL--LARFVIDEAHCVsqWGHDFRPDYKR-LNML- 167
|
170 180 190
....*....|....*....|....*....|.
gi 52782792 197 rdRKTF------LFSATMTKKVQKLQRAALK 221
Cdd:cd18016 168 --RQKFpsvpmmALTATATPRVQKDILNQLK 196
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
254-386 |
1.55e-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: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 254 LVYILNEL--AGNSFMIFcstcnnTQRTALL------LRNLGFTAIPLHGQMSQSKRLGSLNKFKAK--ARSILLATDVA 323
Cdd:COG0553 538 LLELLEELlaEGEKVLVF------SQFTDTLdlleerLEERGIEYAYLHGGTSAEERDELVDRFQEGpeAPVFLISLKAG 611
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52782792 324 SRGLDIPHVDVVVNFDIP---------ThskDYIHRVGRTaragRSGKAITFVTQYDVElfQRIEHLIGKKL 386
Cdd:COG0553 612 GEGLNLTAADHVIHYDLWwnpaveeqaI---DRAHRIGQT----RDVQVYKLVAEGTIE--EKILELLEEKR 674
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
31-214 |
1.63e-04 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350773 [Multi-domain] Cd Length: 209 Bit Score: 42.74 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 31 VTDVLCEaCDQLGWTKPtkIQIEAIPLALQGRDIIGLAETGSGKTGAFALPilnALLEtpqRLFALVLTPTRELafqISE 110
Cdd:cd18015 6 VKDTLKN-VFKLEKFRP--LQLETINATMAGRDVFLVMPTGGGKSLCYQLP---ALCS---DGFTLVVSPLISL---MED 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 111 QFEALGsSIGVQSAVIVGGIDSMSQSLALA---KKP---HIIIATP------GRLIDHLEntKGFNLRALKYLVMDEAD- 177
Cdd:cd18015 74 QLMALK-KLGISATMLNASSSKEHVKWVHAaltDKNselKLLYVTPekiaksKRFMSKLE--KAYNAGRLARIAIDEVHc 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 52782792 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 |
1.67e-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: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 306 LNKFKAKARSILLATDVASRGLDIPHVD--VVVNFDIPTHSKDY---------IHRV-GRTARAGRSGKAI--TFVTQYD 371
Cdd:cd18804 137 LDQFERGEIDILIGTQMIAKGLDFPNVTlvGILNADSGLNSPDFraserafqlLTQVsGRAGRGDKPGKVIiqTYNPEHP 216
|
....*....
gi 52782792 372 veLFQRIEH 380
Cdd:cd18804 217 --LIQAAKE 223
|
|
| Cas3 |
COG1203 |
CRISPR-Cas type I system-associated endonuclease/helicase Cas3 [Defense mechanisms]; ... |
48-329 |
1.40e-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: 40.84 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 48 TKIQIEAIPLALQGRDIIGL-AETGSGKTGAFALPILNALLET-PQRLF-ALvltPTRELAFQISEQF-EALGSSIGVQ- 122
Cdd:COG1203 133 NEALELALEAAEEEPGLFILtAPTGGGKTEAALLFALRLAAKHgGRRIIyAL---PFTSIINQTYDRLrDLFGEDVLLHh 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 123 SAVIV------GGIDSMSQSLALAKK----PhIIIATPGRLIDHLENTKGFNLRAL-----KYLVMDEADrilnmDFETE 187
Cdd:COG1203 210 SLADLdlleeeEEYESEARWLKLLKElwdaP-VVVTTIDQLFESLFSNRKGQERRLhnlanSVIILDEVQ-----AYPPY 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 188 ----VDKILKVIPRDRKTFLF-SATMTkkvqKLQRAALKNPVKCAVSSKYQTVEKLQQYY-----IFIPSKFKDTYLVYI 257
Cdd:COG1203 284 mlalLLRLLEWLKNLGGSVILmTATLP----PLLREELLEAYELIPDEPEELPEYFRAFVrkrveLKEGPLSDEELAELI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 258 LNELA-GNSFMIFCSTCNNTQRTALLLRNLGfTAIP---LHGQMSQSKRLGSLNK----FKAKARSILLATDVASRGLDI 329
Cdd:COG1203 360 LEALHkGKSVLVIVNTVKDAQELYEALKEKL-PDEEvylLHSRFCPADRSEIEKEikerLERGKPCILVSTQVVEAGVDI 438
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
256-364 |
1.44e-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: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 256 YILNELAGNSFMIFCSTCNNTQRTALLLRNLGF-----TAIPLH-GQMSQSKRLGSLNKFKAKARSILLATDVASRGLDI 329
Cdd:cd18796 31 VIFLLERHKSTLVFTNTRSQAERLAQRLRELCPdrvppDFIALHhGSLSRELREEVEAALKRGDLKVVVATSSLELGIDI 110
|
90 100 110
....*....|....*....|....*....|....*
gi 52782792 330 PHVDVVVNFDIPTHSKDYIHRVGrtaRAGRSGKAI 364
Cdd:cd18796 111 GDVDLVIQIGSPKSVARLLQRLG---RSGHRPGAA 142
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
46-178 |
1.60e-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: 39.72 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 46 KPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFA--LVLTPTRELAFQISEQFEALGSSIGVQS 123
Cdd:cd17927 2 KPRNYQLELAQPALKGKNTIICLPTGSGKTFVAVLICEHHLKKFPAGRKGkvVFLANKVPLVEQQKEVFRKHFERPGYKV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 52782792 124 AVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKGFNLRALKYLVMDEADR 178
Cdd:cd17927 82 TGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIVSLSDFSLLVFDECHN 136
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
254-386 |
2.28e-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: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 254 LVYILNELaGNSFMIFCSTCNNTQ---RTALLLRNLGFTAIPLHgqmsqSKRLGSLNKFKAkaRSILLATDVAS------ 324
Cdd:cd18798 16 LLELVKKL-GDGGLIFVSIDYGKEyaeELKEFLERHGIKAELAL-----SSTEKNLEKFEE--GEIDVLIGVASyygvlv 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52782792 325 RGLDIPH-VDVVVNFDIPTHSkdYIHRVGRTAR--AGRSGKAITFVTQYDVELFqrieHLIGKKL 386
Cdd:cd18798 88 RGIDLPErIKYAIFYGVPVTT--YIQASGRTSRlyAGGLTKGLSVVLVDDPELF----EALKKRL 146
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
293-358 |
5.96e-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: 37.25 E-value: 5.96e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 293 LHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIH----RVGRTARAG 358
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIEDADRFGLSQLHqlrgRVGRGKHQS 135
|
|
| DEXHc_RIG-I_DDX58 |
cd18073 |
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called ... |
46-175 |
6.56e-03 |
|
DEXH-box helicase domain of RIG-I; RIG-I (Retinoic acid-inducible gene I protein), also called DEAD box protein 58 (DDX58), is a pathogen-recognition receptor that recognizes viral 5'-triphosphates carrying double-stranded RNA. Upon binding to these microbe-associated molecular patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that result in type I interferon production and induction of an antiviral state. The optimal ligand for RIG-I has been found to be base-paired or double-stranded RNA (dsRNA) molecules containing a 5' triphosphate (5'-ppp-dsRNA). RIG-I contains two N-terminal caspase activation and recruitment domains (CARDs), which are required for interaction with IPS-1, a superfamily 2 helicase/translocase/ATPase (SF2) domain and a C-terminal regulatory/repressor domain (RD). RIG-I is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350831 [Multi-domain] Cd Length: 202 Bit Score: 37.88 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 46 KPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVL-----TPTRELAFQI-SEQFEALGSSI 119
Cdd:cd18073 2 KPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVffatkVPVYEQQKSVfSKYFERHGYRV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 52782792 120 gvqsAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKGFNLRALKYLVMDE 175
Cdd:cd18073 82 ----TGISGATAENVPVEQIIENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDE 133
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
51-179 |
7.07e-03 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 37.27 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 51 QIEAI------PLALQGRDIIGLAeTGSGKTGAFALPILNALLETPQRLFaLVLTPTRELAFQISEQFEALGSSIGVQSA 124
Cdd:pfam04851 8 QIEAIenllesIKNGQKRGLIVMA-TGSGKTLTAAKLIARLFKKGPIKKV-LFLVPRKDLLEQALEEFKKFLPNYVEIGE 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 52782792 125 VIVGgiDSMSQSLALAKkphIIIATPGRLIDHLENTKGFNLR-ALKYLVMDEADRI 179
Cdd:pfam04851 86 IISG--DKKDESVDDNK---IVVTTIQSLYKALELASLELLPdFFDVIIIDEAHRS 136
|
|
| DEXHc_RLR |
cd18036 |
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense ... |
46-159 |
9.95e-03 |
|
DEXH-box helicase domain of RIG-I-like receptors; RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprise RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). RIG-I-like receptors (RLRs) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350794 [Multi-domain] Cd Length: 204 Bit Score: 37.46 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782792 46 KPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETP---QRLFALVLTPTRELAFQISEQFeaLGSSIGVQ 122
Cdd:cd18036 2 ELRNYQLELVLPALRGKNTIICAPTGSGKTRVAVYICRHHLEKRRsagEKGRVVVLVNKVPLVEQQLEKF--FKYFRKGY 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 52782792 123 SAVIVGGIDSMSQSLA-LAKKPHIIIATPGRLIDHLEN 159
Cdd:cd18036 80 KVTGLSGDSSHKVSFGqIVKASDVIICTPQILINNLLS 117
|
|
| |
