|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
188-572 |
1.50e-172 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 498.52 E-value: 1.50e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 188 TFSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQsftqgpspvpaqgggYGRQ 267
Cdd:COG0513 3 SFADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQR---------------LDPS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 268 RKAYPTALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIK 347
Cdd:COG0513 68 RPRAPQALILAPTRELALQVAEELRKLAKYLGLRVATVYGGVSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 348 YLVLDEADRMLDMGFEPQIRRIVqgEDMPPtgQRQTLMFSATFPRDIQMLAQDFLSDYVFLSVGRVGSTSENITQKIEYV 427
Cdd:COG0513 148 TLVLDEADRMLDMGFIEDIERIL--KLLPK--ERQTLLFSATMPPEIRKLAKRYLKNPVRIEVAPENATAETIEQRYYLV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 428 EDIDKRSVLLDILHTHAGGLTLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNGKCPILVATAVAAR 507
Cdd:COG0513 224 DKRDKLELLRRLLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAAR 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 367037389 508 GLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGIATAFFNRGNRGIVReliDLLKEANQEIP 572
Cdd:COG0513 304 GIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLR---AIEKLIGQKIE 365
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
188-414 |
1.80e-164 |
|
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: 470.05 E-value: 1.80e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 188 TFSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTQGPSPVpaqgggYGRQ 267
Cdd:cd17967 1 SFEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPSV------GRGR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 268 RKAYPTALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIK 347
Cdd:cd17967 75 RKAYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVVHQQLQLLRGCDILVATPGRLVDFIERGRISLSSIK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 367037389 348 YLVLDEADRMLDMGFEPQIRRIVQGEDMPPTGQRQTLMFSATFPRDIQMLAQDFLSDYVFLSVGRVG 414
Cdd:cd17967 155 FLVLDEADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLKNYIFLTVGRVG 221
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
167-415 |
2.21e-163 |
|
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: 468.37 E-value: 2.21e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 167 FEKYDDIPVTPSGRDVPEPILTFSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPIL 246
Cdd:cd18051 1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 247 HQSFTQGPSPVPAQGGGYGRQRKAYPTALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLV 326
Cdd:cd18051 81 SQIYEQGPGESLPSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGGADIGQQMRDLERGCHLLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 327 ATPGRLVDLIERGRISLCNIKYLVLDEADRMLDMGFEPQIRRIVQGEDMPPTGQRQTLMFSATFPRDIQMLAQDFLSDYV 406
Cdd:cd18051 161 ATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFLDNYI 240
|
....*....
gi 367037389 407 FLSVGRVGS 415
Cdd:cd18051 241 FLAVGRVGS 249
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
145-414 |
6.48e-141 |
|
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: 411.67 E-value: 6.48e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 145 PRLERELFgtaddpSKQHTGINFEKYDDIPVTPSGRDVPEPILTFSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVING 224
Cdd:cd18052 7 PEDEDEIF------ATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 225 RDLMACAQTGSGKTGGFLFPILHQSFTQGPSPVPAQGGgygrqrkAYPTALILAPTRELVSQIYDEARKFAYRSWVRPCV 304
Cdd:cd18052 81 RDLMACAQTGSGKTAAFLLPVLTGMMKEGLTASSFSEV-------QEPQALIVAPTRELANQIFLEARKFSYGTCIRPVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 305 VYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIKYLVLDEADRMLDMGFEPQIRRIVQGEDMPPTGQRQTL 384
Cdd:cd18052 154 VYGGVSVGHQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTL 233
|
250 260 270
....*....|....*....|....*....|.
gi 367037389 385 MFSATFPRDIQMLAQDFL-SDYVFLSVGRVG 414
Cdd:cd18052 234 MFSATFPEEIQRLAAEFLkEDYLFLTVGRVG 264
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
179-584 |
7.04e-127 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 386.44 E-value: 7.04e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 179 GRDVPEPILTFSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTQgPSPVP 258
Cdd:PTZ00110 122 GENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKTLAFLLPAIVHINAQ-PLLRY 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 259 AQGggygrqrkayPTALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIER 338
Cdd:PTZ00110 201 GDG----------PIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPKRGQIYALRRGVEILIACPGRLIDFLES 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 339 GRISLCNIKYLVLDEADRMLDMGFEPQIRRIVqgEDMPPtgQRQTLMFSATFPRDIQMLAQDFLSDY-VFLSVGRVG-ST 416
Cdd:PTZ00110 271 NVTNLRRVTYLVLDEADRMLDMGFEPQIRKIV--SQIRP--DRQTLMWSATWPKEVQSLARDLCKEEpVHVNVGSLDlTA 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 417 SENITQKIEYVEDIDKRSVLLDILHT--HAGGLTLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNG 494
Cdd:PTZ00110 347 CHNIKQEVFVVEEHEKRGKLKMLLQRimRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTG 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 495 KCPILVATAVAARGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGIATAFFNRGNRGIVRELIDLLKEANQEIPSF 574
Cdd:PTZ00110 427 KSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTPDKYRLARDLVKVLREAKQPVPPE 506
|
410
....*....|
gi 367037389 575 LETIARESSY 584
Cdd:PTZ00110 507 LEKLSNERSN 516
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
189-565 |
1.07e-103 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 323.29 E-value: 1.07e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 189 FSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILH----QSF-TQgpspvpaqggg 263
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQkldvKRFrVQ----------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 264 ygrqrkayptALILAPTRELVSQIYDEARKFAyRSW--VRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRI 341
Cdd:PRK11776 75 ----------ALVLCPTRELADQVAKEIRRLA-RFIpnIKVLTLCGGVPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 342 SLCNIKYLVLDEADRMLDMGFEPQIRRIVqgEDMPPtgQRQTLMFSATFPRDIQMLAQDFLSDYVFLSVGRVGSTSEnIT 421
Cdd:PRK11776 144 DLDALNTLVLDEADRMLDMGFQDAIDAII--RQAPA--RRQTLLFSATYPEGIAAISQRFQRDPVEVKVESTHDLPA-IE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 422 QKIEYVEDIDKRSVLLDILHTHAGGLTLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNGKCPILVA 501
Cdd:PRK11776 219 QRFYEVSPDERLPALQRLLLHHQPESCVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVA 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 367037389 502 TAVAARGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGIATAFFNRGNRGIVRELIDLLK 565
Cdd:PRK11776 299 TDVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPEEMQRANAIEDYLG 362
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
187-572 |
3.97e-96 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 303.65 E-value: 3.97e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 187 LTFSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPIL-----HQSFTQGPSPVpaqg 261
Cdd:PRK10590 1 MSFDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLqhlitRQPHAKGRRPV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 262 ggygrqrkaypTALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRI 341
Cdd:PRK10590 77 -----------RALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGGVSINPQMMKLRGGVDVLVATPGRLLDLEHQNAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 342 SLCNIKYLVLDEADRMLDMGFEPQIRRIVQgeDMPPtgQRQTLMFSATFPRDIQMLAQDFLSDYVFLSVGRVGSTSENIT 421
Cdd:PRK10590 146 KLDQVEILVLDEADRMLDMGFIHDIRRVLA--KLPA--KRQNLLFSATFSDDIKALAEKLLHNPLEIEVARRNTASEQVT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 422 QKIEYVEDIDKRSVLLDILHTHAGGLTLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNGKCPILVA 501
Cdd:PRK10590 222 QHVHFVDKKRKRELLSQMIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVA 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 367037389 502 TAVAARGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGIATAFFNRGNRGIVRELIDLLKeanQEIP 572
Cdd:PRK10590 302 TDIAARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALSLVCVDEHKLLRDIEKLLK---KEIP 369
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
173-572 |
3.04e-94 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 300.55 E-value: 3.04e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 173 IPVTPSGRDVPEPILTFSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFT- 251
Cdd:PLN00206 107 LEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRCCTi 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 252 --QGPSpvpaqgggygRQRKayPTALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATP 329
Cdd:PLN00206 187 rsGHPS----------EQRN--PLAMVLTPTRELCVQVEDQAKVLGKGLPFKTALVVGGDAMPQQLYRIQQGVELIVGTP 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 330 GRLVDLIERGRISLCNIKYLVLDEADRMLDMGFEPQIRRIVQGEDMPptgqrQTLMFSATFPRDIQMLAQDFLSDYVFLS 409
Cdd:PLN00206 255 GRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVMQIFQALSQP-----QVLLFSATVSPEVEKFASSLAKDIILIS 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 410 VGRVGSTSENITQKIEYVEDIDKRSVLLDILHT--HAGGLTLIFVETKRMADSLSDFL-INQNFPATSIHGDRTQRERER 486
Cdd:PLN00206 330 IGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSkqHFKPPAVVFVSSRLGADLLANAItVVTGLKALSIHGEKSMKERRE 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 487 ALELFRNGKCPILVATAVAARGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGIATAFFNRGNRGIVRELIDLLKE 566
Cdd:PLN00206 410 VMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKS 489
|
....*.
gi 367037389 567 ANQEIP 572
Cdd:PLN00206 490 SGAAIP 495
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
189-548 |
5.66e-91 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 290.66 E-value: 5.66e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 189 FSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQsFTQGPSPvpaqgggygRQR 268
Cdd:PRK01297 89 FHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQ-LLQTPPP---------KER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 269 -KAYPTALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIE-RGCDLLVATPGRLVDLIERGRISLCNI 346
Cdd:PRK01297 159 yMGEPRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMDFDKQLKQLEaRFCDILVATPGRLLDFNQRGEVHLDMV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 347 KYLVLDEADRMLDMGFEPQIRRIVQgeDMPPTGQRQTLMFSATFPRDIQMLAQDFLSDYVFLSVGRVGSTSENITQKIEY 426
Cdd:PRK01297 239 EVMVLDEADRMLDMGFIPQVRQIIR--QTPRKEERQTLLFSATFTDDVMNLAKQWTTDPAIVEIEPENVASDTVEQHVYA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 427 VEDIDKRSVLLDILHTHAGGLTLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNGKCPILVATAVAA 506
Cdd:PRK01297 317 VAGSDKYKLLYNLVTQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAG 396
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 367037389 507 RGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGIATAF 548
Cdd:PRK01297 397 RGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
198-409 |
4.47e-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: 278.17 E-value: 4.47e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 198 LLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQsftqgpspVPAQGGGYGRQrkayPTALIL 277
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEK--------LLPEPKKKGRG----PQALVL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 278 APTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIKYLVLDEADRM 357
Cdd:cd00268 69 APTRELAMQIAEVARKLGKGTGLKVAAIYGGAPIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADRM 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 367037389 358 LDMGFEPQIRRIVQgeDMPPtgQRQTLMFSATFPRDIQMLAQDFLSDYVFLS 409
Cdd:cd00268 149 LDMGFEEDVEKILS--ALPK--DRQTLLFSATLPEEVKELAKKFLKNPVRIE 196
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
189-548 |
8.77e-90 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 285.71 E-value: 8.77e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 189 FSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTqgpSPVPAqgggyGRQr 268
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLLS---HPAPE-----DRK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 269 KAYPTALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIKY 348
Cdd:PRK04837 81 VNQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 349 LVLDEADRMLDMGFEPQIRRIVQgeDMPPTGQRQTLMFSATFPRDIQMLAQDFLSDYVFLSVGRVGSTSENITQKIEYVE 428
Cdd:PRK04837 161 VVLDEADRMFDLGFIKDIRWLFR--RMPPANQRLNMLFSATLSYRVRELAFEHMNNPEYVEVEPEQKTGHRIKEELFYPS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 429 DIDKRSVLLDILHTHAGGLTLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNGKCPILVATAVAARG 508
Cdd:PRK04837 239 NEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRGDLDILVATDVAARG 318
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 367037389 509 LDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGIATAF 548
Cdd:PRK04837 319 LHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
188-548 |
1.01e-88 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 283.37 E-value: 1.01e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 188 TFSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILhQSFTQGPspvpaqgggygRQ 267
Cdd:PRK11192 2 TFSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLPAL-QHLLDFP-----------RR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 268 RKAYPTALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIK 347
Cdd:PRK11192 70 KSGPPRILILTPTRELAMQVADQARELAKHTHLDIATITGGVAYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCRAVE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 348 YLVLDEADRMLDMGFEPQIRRIVqGEdmpPTGQRQTLMFSATFP-RDIQMLAQDFLSDYVFLSVGrvGSTSE--NITQKI 424
Cdd:PRK11192 150 TLILDEADRMLDMGFAQDIETIA-AE---TRWRKQTLLFSATLEgDAVQDFAERLLNDPVEVEAE--PSRRErkKIHQWY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 425 EYVEDID-KRSVLLDILHTHAGGLTLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNGKCPILVATA 503
Cdd:PRK11192 224 YRADDLEhKTALLCHLLKQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLTDGRVNVLVATD 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 367037389 504 VAARGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGIATAF 548
Cdd:PRK11192 304 VAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
181-548 |
1.63e-81 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 268.74 E-value: 1.63e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 181 DVPEPILTFSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTQgpspvPAq 260
Cdd:PRK04537 3 DKPLTDLTFSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLLSR-----PA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 261 gggYGRQRKAYPTALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGR 340
Cdd:PRK04537 77 ---LADRKPEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVDYDKQRELLQQGVDVIIATPGRLIDYVKQHK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 341 I-SLCNIKYLVLDEADRMLDMGFEPQIRRIVQgeDMPPTGQRQTLMFSATFPRDIQMLAQDFLSDYVFLSVGRVGSTSEN 419
Cdd:PRK04537 154 VvSLHACEICVLDEADRMFDLGFIKDIRFLLR--RMPERGTRQTLLFSATLSHRVLELAYEHMNEPEKLVVETETITAAR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 420 ITQKIEYVEDIDKRSVLLDILHTHAGGLTLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNGKCPIL 499
Cdd:PRK04537 232 VRQRIYFPADEEKQTLLLGLLSRSEGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEIL 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 367037389 500 VATAVAARGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGIATAF 548
Cdd:PRK04537 312 VATDVAARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISF 360
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
198-409 |
1.31e-74 |
|
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: 238.04 E-value: 1.31e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 198 LLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFP----ILHQsftqgpsPVPAQGGGygrqrkayPT 273
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLPaivhINAQ-------PPLERGDG--------PI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 274 ALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIKYLVLDE 353
Cdd:cd17966 66 VLVLAPTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGPQIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 367037389 354 ADRMLDMGFEPQIRRIVqGEDMPptgQRQTLMFSATFPRDIQMLAQDFLSDYVFLS 409
Cdd:cd17966 146 ADRMLDMGFEPQIRKIV-DQIRP---DRQTLMWSATWPKEVRRLAEDFLKDYIQVN 197
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
188-565 |
3.36e-69 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 237.44 E-value: 3.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 188 TFSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQsftqgpspvpaqgggYGRQ 267
Cdd:PRK11634 7 TFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHN---------------LDPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 268 RKAyPTALILAPTRELVSQIYDEARKFA-YRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNI 346
Cdd:PRK11634 72 LKA-PQILVLAPTRELAVQVAEAMTDFSkHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 347 KYLVLDEADRMLDMGFEPQIRRIVQgeDMPptGQRQTLMFSATFPRDIQMLAQDFLSDYVFLSVGRVGSTSENITQKIEY 426
Cdd:PRK11634 151 SGLVLDEADEMLRMGFIEDVETIMA--QIP--EGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 427 VEDIDKRSVLLDILHTHAGGLTLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNGKCPILVATAVAA 506
Cdd:PRK11634 227 VWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAA 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 367037389 507 RGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGIATAFFNRGNRGIVRELIDLLK 565
Cdd:PRK11634 307 RGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMK 365
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
178-404 |
1.04e-67 |
|
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: 220.71 E-value: 1.04e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 178 SGRDVPEPILTFSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTQgPSPV 257
Cdd:cd17953 3 RGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKDQ-RPVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 258 PAQGggygrqrkayPTALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLI- 336
Cdd:cd17953 82 PGEG----------PIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGGSGISEQIAELKRGAEIVVCTPGRMIDILt 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 337 -ERGRI-SLCNIKYLVLDEADRMLDMGFEPQIRRIVQgeDMPPtgQRQTLMFSATFPRDIQMLAQDFLSD 404
Cdd:cd17953 152 aNNGRVtNLRRVTYVVLDEADRMFDMGFEPQIMKIVN--NIRP--DRQTVLFSATFPRKVEALARKVLHK 217
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
175-411 |
5.85e-66 |
|
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: 216.80 E-value: 5.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 175 VTPSGRDVPEPILTFSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFP----ILHQSF 250
Cdd:cd18049 12 ITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPaivhINHQPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 251 TQgpspvpaQGGGygrqrkayPTALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPG 330
Cdd:cd18049 92 LE-------RGDG--------PICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 331 RLVDLIERGRISLCNIKYLVLDEADRMLDMGFEPQIRRIVqgEDMPPtgQRQTLMFSATFPRDIQMLAQDFLSDYVFLSV 410
Cdd:cd18049 157 RLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIV--DQIRP--DRQTLMWSATWPKEVRQLAEDFLKDYIHINI 232
|
.
gi 367037389 411 G 411
Cdd:cd18049 233 G 233
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
420-549 |
4.68e-64 |
|
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: 207.75 E-value: 4.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 420 ITQKIEYVEDIDKRSVLL-DILHTHAGGLTLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNGKCPI 498
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLlLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 367037389 499 LVATAVAARGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGIATAFF 549
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
198-404 |
2.29e-63 |
|
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: 208.42 E-value: 2.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 198 LLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTQgPSPVPAQGggygrqrkayPTALIL 277
Cdd:cd17952 1 LLNAIRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIMDQ-RELEKGEG----------PIAVIV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 278 APTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIKYLVLDEADRM 357
Cdd:cd17952 70 APTRELAQQIYLEAKKFGKAYNLRVVAVYGGGSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRM 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 367037389 358 LDMGFEPQIRRIVqGEDMPptgQRQTLMFSATFPRDIQMLAQDFLSD 404
Cdd:cd17952 150 FDMGFEYQVRSIV-GHVRP---DRQTLLFSATFKKKIEQLARDILSD 192
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
175-411 |
1.33e-60 |
|
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: 203.70 E-value: 1.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 175 VTPSGRDVPEPILTFSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFP----ILHQSF 250
Cdd:cd18050 50 ITIRGVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPaivhINHQPY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 251 TQgpspvpaQGGGygrqrkayPTALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPG 330
Cdd:cd18050 130 LE-------RGDG--------PICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPKGPQIRDLERGVEICIATPG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 331 RLVDLIERGRISLCNIKYLVLDEADRMLDMGFEPQIRRIVqgEDMPPtgQRQTLMFSATFPRDIQMLAQDFLSDYVFLSV 410
Cdd:cd18050 195 RLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIV--DQIRP--DRQTLMWSATWPKEVRQLAEDFLRDYVQINI 270
|
.
gi 367037389 411 G 411
Cdd:cd18050 271 G 271
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
198-411 |
5.61e-60 |
|
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: 199.35 E-value: 5.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 198 LLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQsftqgpspvpaqgggYGRQRKAY-PTALI 276
Cdd:cd17957 1 LLNNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQK---------------LGKPRKKKgLRALI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 277 LAPTRELVSQIYDEARKFAYRSWVRPCVVYGG-ADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIKYLVLDEAD 355
Cdd:cd17957 66 LAPTRELASQIYRELLKLSKGTGLRIVLLSKSlEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEAD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 367037389 356 RMLDMGFEPQIRRIVQGEDMPptgQRQTLMFSATFPRDIQMLAQDFLSDYVFLSVG 411
Cdd:cd17957 146 KLFEPGFREQTDEILAACTNP---NLQRSLFSATIPSEVEELARSVMKDPIRIIVG 198
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
198-409 |
8.55e-60 |
|
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: 199.85 E-value: 8.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 198 LLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILhQSFTQGPsPVPAQGGGYGrqrkayPTALIL 277
Cdd:cd17945 1 LLRVIRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLL-VYISRLP-PLDEETKDDG------PYALIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 278 APTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIKYLVLDEADRM 357
Cdd:cd17945 73 APTRELAQQIEEETQKFAKPLGIRVVSIVGGHSIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 358 LDMGFEPQIRRIVqgEDMPPTG------------------QRQTLMFSATFPRDIQMLAQDFLSDYVFLS 409
Cdd:cd17945 153 IDMGFEPQVTKIL--DAMPVSNkkpdteeaeklaasgkhrYRQTMMFTATMPPAVEKIAKGYLRRPVVVT 220
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
184-548 |
2.08e-59 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 205.06 E-value: 2.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 184 EPILTFSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSftqGPSPVPAQggg 263
Cdd:PTZ00424 25 EIVDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVIAALQLI---DYDLNACQ--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 264 ygrqrkayptALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISL 343
Cdd:PTZ00424 99 ----------ALILAPTRELAQQIQKVVLALGDYLKVRCHACVGGTVVRDDINKLKAGVHMVVGTPGRVYDMIDKRHLRV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 344 CNIKYLVLDEADRMLDMGFEPQIRRIVQgeDMPPtgQRQTLMFSATFPRDIQMLAQDFLSDYVFLSVGRVGSTSENITQK 423
Cdd:PTZ00424 169 DDLKLFILDEADEMLSRGFKGQIYDVFK--KLPP--DVQVALFSATMPNEILELTTKFMRDPKRILVKKDELTLEGIRQF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 424 IEYVEDID-KRSVLLDILHTHAGGLTLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNGKCPILVAT 502
Cdd:PTZ00424 245 YVAVEKEEwKFDTLCDLYETLTITQAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITT 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 367037389 503 AVAARGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGIATAF 548
Cdd:PTZ00424 325 DLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINF 370
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
194-409 |
2.37e-58 |
|
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: 195.49 E-value: 2.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 194 LDPHLLSNIELARYKIPTPVQKYSIPIVI-NGRDLMACAQTGSGKTGGFLFPILHQSFTQGPSPVPAQGGgygrqrkayp 272
Cdd:cd17964 1 LDPSLLKALTRMGFETMTPVQQKTLKPILsTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGVS---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 273 tALILAPTRELVSQIYDEARKF-AYRSWVRPCVVYGGADIGSQLRQIER-GCDLLVATPGRLVDLIE--RGRISLCNIKY 348
Cdd:cd17964 71 -ALIISPTRELALQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRRgRPDILVATPGRLIDHLEnpGVAKAFTDLDY 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 367037389 349 LVLDEADRMLDMGFEPQIRRIVQGEDMPPTGQRQTLMFSATFPRDIQMLAQDFL-SDYVFLS 409
Cdd:cd17964 150 LVLDEADRLLDMGFRPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLkKDYKFID 211
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
211-397 |
1.14e-57 |
|
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: 192.07 E-value: 1.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 211 TPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSftqgpspvpaqgggygRQRKAYPTALILAPTRELVSQIYDE 290
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL----------------DKLDNGPQALVLAPTRELAEQIYEE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 291 ARKFAYRSWVRPCVVYGGADIGSQLRQIeRGCDLLVATPGRLVDLI-ERGRISlcNIKYLVLDEADRMLDMGFEPQIRRI 369
Cdd:pfam00270 65 LKKLGKGLGLKVASLLGGDSRKEQLEKL-KGPDILVGTPGRLLDLLqERKLLK--NLKLLVLDEAHRLLDMGFGPDLEEI 141
|
170 180
....*....|....*....|....*...
gi 367037389 370 VqgEDMPPtgQRQTLMFSATFPRDIQML 397
Cdd:pfam00270 142 L--RRLPK--KRQILLLSATLPRNLEDL 165
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
202-423 |
2.82e-55 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 186.93 E-value: 2.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 202 IELARYKIPTPVQKYSIPIVING-RDLMACAQTGSGKTGGFLFPILHQsftqgpspvpaqgggygRQRKAYPTALILAPT 280
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEA-----------------LKRGKGGRVLVLVPT 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 281 RELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGC-DLLVATPGRLVDLIERGRISLCNIKYLVLDEADRMLD 359
Cdd:smart00487 64 RELAEQWAEELKKLGPSLGLKVVGLYGGDSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 367037389 360 MGFEPQIRRIVQgeDMPPtgQRQTLMFSATFPRDIQMLAQDFLSDYVFLSVGRvgSTSENITQK 423
Cdd:smart00487 144 GGFGDQLEKLLK--LLPK--NVQLLLLSATPPEEIENLLELFLNDPVFIDVGF--TPLEPIEQF 201
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
198-404 |
4.96e-55 |
|
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: 186.13 E-value: 4.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 198 LLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTQgPSPvpaqgggygRQRKAYPTALIL 277
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPGFIHLDLQ-PIP---------REQRNGPGVLVL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 278 APTRELVSQIYDEARKFAYRSWVRPCVvYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIKYLVLDEADRM 357
Cdd:cd17958 71 TPTRELALQIEAECSKYSYKGLKSVCV-YGGGNRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEADRM 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 367037389 358 LDMGFEPQIRRIVQgeDMPPtgQRQTLMFSATFPRDIQMLAQDFLSD 404
Cdd:cd17958 150 LDMGFEPQIRKILL--DIRP--DRQTIMTSATWPDGVRRLAQSYLKD 192
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
207-398 |
5.02e-55 |
|
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: 186.31 E-value: 5.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 207 YKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSftqgpspvpaqggGYGRQRKAYPTALILAPTRELVSQ 286
Cdd:cd17947 10 FTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPILERL-------------LYRPKKKAATRVLVLVPTRELAMQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 287 IYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGR-ISLCNIKYLVLDEADRMLDMGFEPQ 365
Cdd:cd17947 77 CFSVLQQLAQFTDITFALAVGGLSLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLEEGFADE 156
|
170 180 190
....*....|....*....|....*....|...
gi 367037389 366 IRRIVQgedMPPtGQRQTLMFSATFPRDIQMLA 398
Cdd:cd17947 157 LKEILR---LCP-RTRQTMLFSATMTDEVKDLA 185
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
197-409 |
1.38e-53 |
|
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: 182.79 E-value: 1.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 197 HLLSNIELARykiPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTQgPSPVpaqgggygrQRKAYPTALI 276
Cdd:cd17949 4 HLKSKMGIEK---PTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSL-EPRV---------DRSDGTLALV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 277 LAPTRELVSQIYDEARKF-AYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGR-ISLCNIKYLVLDEA 354
Cdd:cd17949 71 LVPTRELALQIYEVLEKLlKPFHWIVPGYLIGGEKRKSEKARLRKGVNILIATPGRLLDHLKNTQsFDVSNLRWLVLDEA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 367037389 355 DRMLDMGFEPQIRRIVQ---------GEDMPPTGQRQTLMFSATFPRDIQMLAQDFLSDYVFLS 409
Cdd:cd17949 151 DRLLDMGFEKDITKILEllddkrskaGGEKSKPSRRQTVLVSATLTDGVKRLAGLSLKDPVYID 214
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
194-408 |
2.98e-52 |
|
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: 179.04 E-value: 2.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 194 LDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQsfTQGPSPvpaQGGGygrqrkaypT 273
Cdd:cd17959 8 LSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEK--LKAHSP---TVGA---------R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 274 ALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIKYLVLDE 353
Cdd:cd17959 74 ALILSPTRELALQTLKVTKELGKFTDLRTALLVGGDSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVEYVVFDE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 367037389 354 ADRMLDMGFEPQIRRIVQgeDMPPTgqRQTLMFSATFPRDIQMLAQDFLSDYVFL 408
Cdd:cd17959 154 ADRLFEMGFAEQLHEILS--RLPEN--RQTLLFSATLPKLLVEFAKAGLNEPVLI 204
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
208-408 |
5.94e-51 |
|
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts with several spliceosomal proteins and may recognize the bacterial second messengers cyclic di-GMP and cyclic di-AMP, resulting in the induction of genes involved in the innate immune response. Diseases associated with DDX41 include "myeloproliferative/lymphoproliferative neoplasms, familial" and "Ddx41-related susceptibility to familial myeloproliferative/lymphoproliferative neoplasms". DDX41 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350709 [Multi-domain] Cd Length: 206 Bit Score: 175.61 E-value: 5.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 208 KIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTQGPSPVPAQGGGygrqrkayPTALILAPTRELVSQI 287
Cdd:cd17951 11 KKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALEQEKKLPFIKGEG--------PYGLIVCPSRELARQT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 288 YDEARKFAYR------SWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIKYLVLDEADRMLDMG 361
Cdd:cd17951 83 HEVIEYYCKAlqeggyPQLRCLLCIGGMSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEADRMIDMG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 367037389 362 FEPQIRRIVQGEdmppTGQRQTLMFSATFPRDIQMLAQDFLSDYVFL 408
Cdd:cd17951 163 FEEDIRTIFSYF----KGQRQTLLFSATMPKKIQNFAKSALVKPVTV 205
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
188-406 |
3.37e-50 |
|
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: 173.27 E-value: 3.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 188 TFSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILhQSFTQGPSPVpaqgggygrq 267
Cdd:cd17954 1 TFKELGVCEELCEACEKLGWKKPTKIQEEAIPVALQGRDIIGLAETGSGKTAAFALPIL-QALLENPQRF---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 268 rkaypTALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGR-ISLCNI 346
Cdd:cd17954 70 -----FALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAIALAKKPHVIVATPGRLVDHLENTKgFSLKSL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 347 KYLVLDEADRMLDMGFEPQIRRIVqgEDMPPtgQRQTLMFSATFPRDIQMLAQDFLSDYV 406
Cdd:cd17954 145 KFLVMDEADRLLNMDFEPEIDKIL--KVIPR--ERTTYLFSATMTTKVAKLQRASLKNPV 200
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
198-409 |
7.57e-48 |
|
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: 166.57 E-value: 7.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 198 LLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTQGPSPvpaqgggygrqrkaypTALIL 277
Cdd:cd17962 1 LSSNLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLTEHRNP----------------SALIL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 278 APTRELVSQIYDEARKFAY-RSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIKYLVLDEADR 356
Cdd:cd17962 65 TPTRELAVQIEDQAKELMKgLPPMKTALLVGGLPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADT 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 367037389 357 MLDMGFEPQIRRIVQGedmpPTGQRQTLMFSATFPRDIQMLAQDFLSDYVFLS 409
Cdd:cd17962 145 MLKMGFQQQVLDILEN----ISHDHQTILVSATIPRGIEQLAGQLLQNPVRIT 193
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
189-409 |
2.59e-47 |
|
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: 165.48 E-value: 2.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 189 FSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQsFTQGPspvpaqgggYGrqr 268
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQR-LSEDP---------YG--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 269 kayPTALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIE---RGRISLCN 345
Cdd:cd17955 68 ---IFALVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVKQALELSKRPHIVVATPGRLADHLRssdDTTKVLSR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 367037389 346 IKYLVLDEADRMLDMGFEPQIRRIVqgEDMPPtgQRQTLMFSATFPRDIQMLAQDFLSDYVFLS 409
Cdd:cd17955 145 VKFLVLDEADRLLTGSFEDDLATIL--SALPP--KRQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
205-410 |
2.14e-45 |
|
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: 160.15 E-value: 2.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 205 ARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTQGPSPvpaqGGGYGrqrkayptALILAPTRELV 284
Cdd:cd17941 8 AGFIKMTEIQRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLEKLYRERWTP----EDGLG--------ALIISPTRELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 285 SQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERgCDLLVATPGRLVD-LIERGRISLCNIKYLVLDEADRMLDMGFE 363
Cdd:cd17941 76 MQIFEVLRKVGKYHSFSAGLIIGGKDVKEEKERINR-MNILVCTPGRLLQhMDETPGFDTSNLQMLVLDEADRILDMGFK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 367037389 364 PQIRRIVqgEDMPPtgQRQTLMFSATFPRDIQMLAQDFLSDYVFLSV 410
Cdd:cd17941 155 ETLDAIV--ENLPK--SRQTLLFSATQTKSVKDLARLSLKNPEYISV 197
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
196-389 |
5.23e-43 |
|
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: 154.02 E-value: 5.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 196 PHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHqsftqgpspvpaqgggygrqrkaYPTAL 275
Cdd:cd17938 8 PELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVLQ-----------------------IVVAL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 276 ILAPTRELVSQIYDEARKFAY---RSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIKYLVLD 352
Cdd:cd17938 65 ILEPSRELAEQTYNCIENFKKyldNPKLRVALLIGGVKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLSSVRFFVLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 367037389 353 EADRMLDMGFEPQIRRIVqgEDMP---PTGQR-QTLMFSAT 389
Cdd:cd17938 145 EADRLLSQGNLETINRIY--NRIPkitSDGKRlQVIVCSAT 183
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
206-434 |
1.12e-42 |
|
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: 153.93 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 206 RYKIPTPVQKYSIP-IVINGRDLMACAQTGSGKTGGFLFPILHQSFTQgpspvPAQGGGYGRQRkaYPTALILAPTRELV 284
Cdd:cd17946 9 GFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLSQ-----KSSNGVGGKQK--PLRALILTPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 285 SQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCN---IKYLVLDEADRMLDMG 361
Cdd:cd17946 82 VQVKDHLKAIAKYTNIKIASIVGGLAVQKQERLLKKRPEIVVATPGRLWELIQEGNEHLANlksLRFLVLDEADRMLEKG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 367037389 362 -FEP--QIRRIVQGEDMPPTGQRQTLMFSATFPRDIQMLAQdflsdyvflSVGRVGSTSENITQKIEY-VEDIDKRS 434
Cdd:cd17946 162 hFAEleKILELLNKDRAGKKRKRQTFVFSATLTLDHQLPLK---------LNSKKKKKKKEKKQKLELlIEKVGFRK 229
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
431-540 |
1.77e-42 |
|
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: 148.90 E-value: 1.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 431 DKRSVLLDILHTHAGGLTLIFVETKRMADsLSDFLINQNFPATSIHGDRTQRERERALELFRNGKCPILVATAVAARGLD 510
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 367037389 511 IPNVTHVINYDLPTDIDDYVHRIGRTGRAG 540
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
194-402 |
6.45e-42 |
|
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: 150.91 E-value: 6.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 194 LDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTQgpspvpaqgggygrqrKAYPT 273
Cdd:cd17940 6 LKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDPK----------------KDVIQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 274 ALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIKYLVLDE 353
Cdd:cd17940 70 ALILVPTRELALQTSQVCKELGKHMGVKVMVTTGGTSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCKTLVLDE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 367037389 354 ADRMLDMGFEPQIRRIVQgeDMPPtgQRQTLMFSATFPRDIQMLAQDFL 402
Cdd:cd17940 150 ADKLLSQDFQPIIEKILN--FLPK--ERQILLFSATFPLTVKNFMDRHM 194
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
207-402 |
1.95e-40 |
|
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: 146.57 E-value: 1.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 207 YKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILhQSFTQgpspvpaqggGYGRQRKAYPTALILAPTRELVSQ 286
Cdd:cd17960 10 FTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVL-EILLK----------RKANLKKGQVGALIISPTRELATQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 287 IYDEARKFAYRSW--VRPCVVYGGADIGSQLRQIER-GCDLLVATPGRLVDLIERGRISLC--NIKYLVLDEADRMLDMG 361
Cdd:cd17960 79 IYEVLQSFLEHHLpkLKCQLLIGGTNVEEDVKKFKRnGPNILVGTPGRLEELLSRKADKVKvkSLEVLVLDEADRLLDLG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 367037389 362 FEPQIRRIVqgEDMPPtgQRQTLMFSATFPRDIQMLAQDFL 402
Cdd:cd17960 159 FEADLNRIL--SKLPK--QRRTGLFSATQTDAVEELIKAGL 195
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
194-408 |
5.87e-40 |
|
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: 145.42 E-value: 5.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 194 LDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTQGPSPVPAQGggygrqrkayPT 273
Cdd:cd17961 1 LDPRLLKAIAKLGWEKPTLIQSKAIPLALEGKDILARARTGSGKTAAYALPIIQKILKAKAESGEEQG----------TR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 274 ALILAPTRELVSQIYDEARKFAY--RSWVRpCV-VYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLC-NIKYL 349
Cdd:cd17961 71 ALILVPTRELAQQVSKVLEQLTAycRKDVR-VVnLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGSLLLLsTLKYL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 367037389 350 VLDEADRMLDMGFEPQIRRIVQgedMPPTGqRQTLMFSATFPRDIQMLAQDFLSDYVFL 408
Cdd:cd17961 150 VIDEADLVLSYGYEEDLKSLLS---YLPKN-YQTFLMSATLSEDVEALKKLVLHNPAIL 204
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
211-398 |
1.01e-35 |
|
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: 133.25 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 211 TPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTQGPSPVPAQGggygrqrkayptALILAPTRELVSQIYDE 290
Cdd:cd17942 14 TEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELLYKLKFKPRNGTG------------VIIISPTRELALQIYGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 291 ARKF-AYRSWVRPCVVyGGADIGSQLRQIERGCDLLVATPGRLVD-LIERGRISLCNIKYLVLDEADRMLDMGFEPQIRR 368
Cdd:cd17942 82 AKELlKYHSQTFGIVI-GGANRKAEAEKLGKGVNILVATPGRLLDhLQNTKGFLYKNLQCLIIDEADRILEIGFEEEMRQ 160
|
170 180 190
....*....|....*....|....*....|
gi 367037389 369 IVQgedMPPTgQRQTLMFSATFPRDIQMLA 398
Cdd:cd17942 161 IIK---LLPK-RRQTMLFSATQTRKVEDLA 186
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
212-402 |
8.10e-35 |
|
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: 131.12 E-value: 8.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 212 PVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQsftqgpspvpAQGGGYGRQRKAYPTALILAPTRELVSQIYDEA 291
Cdd:cd17944 15 PIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEK----------LQEDQQPRKRGRAPKVLVLAPTRELANQVTKDF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 292 RKFAYRSWVrpCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIKYLVLDEADRMLDMGFEPQIRRIVQ 371
Cdd:cd17944 85 KDITRKLSV--ACFYGGTPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQMLDMGFAEQVEEILS 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 367037389 372 ------GEDMPptgqrQTLMFSATFPRDIQMLAQDFL 402
Cdd:cd17944 163 vsykkdSEDNP-----QTLLFSATCPDWVYNVAKKYM 194
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
194-404 |
8.57e-35 |
|
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: 130.93 E-value: 8.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 194 LDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSftqgpSPVPAQgggygrqrkayPT 273
Cdd:cd17950 9 LKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQL-----EPVDGQ-----------VS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 274 ALILAPTRELVSQIYDEARKFA-YRSWVRPCVVYGGADIGSQLRQIERGC-DLLVATPGRLVDLIERGRISLCNIKYLVL 351
Cdd:cd17950 73 VLVICHTRELAFQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCpHIVVGTPGRILALVREKKLKLSHVKHFVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 367037389 352 DEADRM---LDMgfepqiRRIVQGEDMPPTGQRQTLMFSATFPRDIQMLAQDFLSD 404
Cdd:cd17950 153 DECDKMleqLDM------RRDVQEIFRATPHDKQVMMFSATLSKEIRPVCKKFMQD 202
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
194-408 |
3.93e-34 |
|
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: 128.85 E-value: 3.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 194 LDPHLLSNIELARYKIPTPVQKYSIPIVING--RDLMACAQTGSGKTGGFLFPILhqsftqgpSPVPAqgggygrqRKAY 271
Cdd:cd17963 1 LKPELLKGLYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAML--------SRVDP--------TLKS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 272 PTALILAPTRELVSQIYDEARKFA------YRSWVRPCVVYGGADIGSQLrqiergcdlLVATPGRLVDLIERGRISLCN 345
Cdd:cd17963 65 PQALCLAPTRELARQIGEVVEKMGkftgvkVALAVPGNDVPRGKKITAQI---------VIGTPGTVLDWLKKRQLDLKK 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 367037389 346 IKYLVLDEADRMLDM-GFEPQIRRIVQgeDMPPtgQRQTLMFSATFPRDIQMLAQDFLSDYVFL 408
Cdd:cd17963 136 IKILVLDEADVMLDTqGHGDQSIRIKR--MLPR--NCQILLFSATFPDSVRKFAEKIAPNANTI 195
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
193-406 |
1.02e-33 |
|
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: 127.83 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 193 PLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTQGPSPvpaqgggygrqrkayp 272
Cdd:cd17939 3 GLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDTTVRET---------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 273 TALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIKYLVLD 352
Cdd:cd17939 67 QALVLAPTRELAQQIQKVVKALGDYMGVKVHACIGGTSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMFVLD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 367037389 353 EADRMLDMGFEPQIRRIVQgedMPPTgQRQTLMFSATFPRDIQMLAQDFLSDYV 406
Cdd:cd17939 147 EADEMLSRGFKDQIYDIFQ---FLPP-ETQVVLFSATMPHEVLEVTKKFMRDPV 196
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
189-406 |
3.69e-33 |
|
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: 126.41 E-value: 3.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 189 FSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTQGPSPvpaqgggygrqr 268
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSLKAT------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 269 kaypTALILAPTRELVSQI---------YDEARkfayrswVRPCVvyGGADIGSQLRQIERGCDLLVATPGRLVDLIERG 339
Cdd:cd18046 69 ----QALVLAPTRELAQQIqkvvmalgdYMGIK-------CHACI--GGTSVRDDAQKLQAGPHIVVGTPGRVFDMINRR 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 367037389 340 RISLCNIKYLVLDEADRMLDMGFEPQIRRIVQgeDMPPTgqRQTLMFSATFPRDIQMLAQDFLSDYV 406
Cdd:cd18046 136 YLRTDYIKMFVLDEADEMLSRGFKDQIYDIFQ--KLPPD--TQVVLLSATMPNDVLEVTTKFMRDPI 198
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
459-540 |
1.44e-31 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 117.31 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 459 DSLSDFLINQNFPATSIHGDRTQRERERALELFRNGKCPILVATAVAARGLDIPNVTHVINYDLPTDIDDYVHRIGRTGR 538
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 367037389 539 AG 540
Cdd:smart00490 81 AG 82
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
210-409 |
1.46e-30 |
|
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: 118.52 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 210 PTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSftqgpspvpaqgggygRQRKAYPTALILAPTRELVSQIYD 289
Cdd:cd17943 13 PSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVIALESL----------------DLERRHPQVLILAPTREIAVQIHD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 290 EARKFA-YRSWVRPCVVYGGADIgSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIKYLVLDEADRMLDMGFEPQIRR 368
Cdd:cd17943 77 VFKKIGkKLEGLKCEVFIGGTPV-KEDKKKLKGCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKLMEGSFQKDVNW 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 367037389 369 IVqgEDMPptGQRQTLMFSATFPRDIQMLAQDFLSDYVFLS 409
Cdd:cd17943 156 IF--SSLP--KNKQVIAFSATYPKNLDNLLARYMRKPVLVR 192
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
198-427 |
2.59e-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: 119.01 E-value: 2.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 198 LLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTQGPSPvpaqgggyGRQRKAyPTALIL 277
Cdd:cd17948 1 LVEILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRYKLLA--------EGPFNA-PRGLVI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 278 APTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGsQLRQIERG-CDLLVATPGRLVDLIERGRISLCNIKYLVLDEADR 356
Cdd:cd17948 72 TPSRELAEQIGSVAQSLTEGLGLKVKVITGGRTKR-QIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 357 MLDMGFEPQIRRI-----VQGEDMPPTGQR----QTLMFSATFPRDiqmlAQDFLSDyvflsVGRVGSTSENITQKIEYV 427
Cdd:cd17948 151 LLDDSFNEKLSHFlrrfpLASRRSENTDGLdpgtQLVLVSATMPSG----VGEVLSK-----VIDVDSIETVTSDKLHRL 221
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
189-406 |
1.48e-29 |
|
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor 4A-III (EIF4AIII, also known as DDX48) is part of the exon junction complex (EJC) that plays a major role in posttranscriptional regulation of mRNA. EJC consists of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. DDX48 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350803 [Multi-domain] Cd Length: 201 Bit Score: 116.03 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 189 FSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKTGGFLFPILHQSFTQgpspvpaqgggygrQR 268
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQ--------------VR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 269 KayPTALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLCNIKY 348
Cdd:cd18045 67 E--TQALILSPTRELAVQIQKVLLALGDYMNVQCHACIGGTSVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIKM 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 367037389 349 LVLDEADRMLDMGFEPQIRRIVQGedMPPTgqRQTLMFSATFPRDIQMLAQDFLSDYV 406
Cdd:cd18045 145 LVLDEADEMLNKGFKEQIYDVYRY--LPPA--TQVVLVSATLPQDILEMTNKFMTDPI 198
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
198-399 |
3.46e-29 |
|
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: 115.81 E-value: 3.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 198 LLSNIELARYKIPTPVQKYSIPIVING---------RDLMACAQTGSGKTGGFLFPILhQSFTQGPSPvpaqgggygRQR 268
Cdd:cd17956 1 LLKNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIV-QALSKRVVP---------RLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 269 kayptALILAPTRELVSQIYDEARKFAYRSWVRPCVVYGGADI---GSQLRQIERG-----CDLLVATPGRLVDLIERGR 340
Cdd:cd17956 71 -----ALIVVPTKELVQQVYKVFESLCKGTGLKVVSLSGQKSFkkeQKLLLVDTSGrylsrVDILVATPGRLVDHLNSTP 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 367037389 341 -ISLCNIKYLVLDEADRMLDMGF----EPQIRRIVQGEDM------------PPTGQRQTLMFSATFPRDIQMLAQ 399
Cdd:cd17956 146 gFTLKHLRFLVIDEADRLLNQSFqdwlETVMKALGRPTAPdlgsfgdanlleRSVRPLQKLLFSATLTRDPEKLSS 221
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
315-562 |
1.59e-25 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 110.62 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 315 LRQIERG-CDLLVATPGRL-----VDLIERGRISLcnikyLVLDEA--------DrmldmgFEP---QIRRIVQGEDMPP 377
Cdd:COG0514 100 LRALRAGeLKLLYVAPERLlnprfLELLRRLKISL-----FAIDEAhcisqwghD------FRPdyrRLGELRERLPNVP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 378 TgqrqtLMFSATFPRDIQ--MLAQDFLSD-YVFL-SVGRvgstsENITQKIEYVEDIDKRSVLLDILHTHAGGLTLIFVE 453
Cdd:COG0514 169 V-----LALTATATPRVRadIAEQLGLEDpRVFVgSFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPGGSGIVYCL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 454 TKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNGKCPILVATaVA-ARGLDIPNVTHVINYDLPTDIDDYVHR 532
Cdd:COG0514 239 SRKKVEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQE 317
|
250 260 270
....*....|....*....|....*....|
gi 367037389 533 IGRTGRAGNTGIATAFFNRGNRGIVRELID 562
Cdd:COG0514 318 IGRAGRDGLPAEALLLYGPEDVAIQRFFIE 347
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
223-518 |
3.40e-24 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 107.42 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 223 NGRDLMACAQTGSGKTGGFLFPIlhqsftqgpspvpaqgggygRQRKAYPTALILAPTRELVSQIYDEARKFAyrswvrp 302
Cdd:COG1061 99 GGGRGLVVAPTGTGKTVLALALA--------------------AELLRGKRVLVLVPRRELLEQWAEELRRFL------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 303 cvvyggADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLcNIKYLVLDEADRmldmGFEPQIRRIVqgEDMPPtgqRQ 382
Cdd:COG1061 152 ------GDPLAGGGKKDSDAPITVATYQSLARRAHLDELGD-RFGLVIIDEAHH----AGAPSYRRIL--EAFPA---AY 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 383 TLMFSATFPRD-------------------IQMLAQDFLSDYVFLSV--------GRVGSTSENITQKIEYVEDIdKRSV 435
Cdd:COG1061 216 RLGLTATPFRSdgreillflfdgivyeyslKEAIEDGYLAPPEYYGIrvdltderAEYDALSERLREALAADAER-KDKI 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 436 LLDILHTHAGGL-TLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNGKCPILVATAVAARGLDIPNV 514
Cdd:COG1061 295 LRELLREHPDDRkTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVPRL 374
|
....
gi 367037389 515 THVI 518
Cdd:COG1061 375 DVAI 378
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
170-392 |
2.27e-19 |
|
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: 88.20 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 170 YDDIPVTPSGRD-VPEPILTFSNPPLDphllsnielarYKIPTPVQKYSIPIvINGRDL-----------------MACA 231
Cdd:cd17965 1 FDQLKLLPSVREaIIKEILKGSNKTDE-----------EIKPSPIQTLAIKK-LLKTLMrkvtkqtsneepklevfLLAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 232 QTGSGKTGGFLFPIL-------HQSFTQGPSPVPaqgggyGRQRKAYPTALILAPTRELVSQIYDEARKFAYRSWVRPCV 304
Cdd:cd17965 69 ETGSGKTLAYLAPLLdylkrqeQEPFEEAEEEYE------SAKDTGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 305 VygGADIGSQLRQIER----GCDLLVATPGRLVDLIERGRISLCNIKYLVLDEADRMLDMGFEPQIRRIVqgEDMPPTGQ 380
Cdd:cd17965 143 F--SSGFGPSYQRLQLafkgRIDILVTTPGKLASLAKSRPKILSRVTHLVVDEADTLFDRSFLQDTTSII--KRAPKLKH 218
|
250
....*....|...
gi 367037389 381 rqtLMF-SATFPR 392
Cdd:cd17965 219 ---LILcSATIPK 228
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
398-570 |
6.31e-19 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 91.33 E-value: 6.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 398 AQDFLSDYVFLSVGRVGSTSENITQKIEYVedidkRSVLLDILHTHAGGLTLIFVETKRMADSLSDFLINQNFPAT---- 473
Cdd:COG1111 311 SKRLVSDPRFRKAMRLAEEADIEHPKLSKL-----REILKEQLGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGrfvg 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 474 --SIHGDR--TQRERERALELFRNGKCPILVATAVAARGLDIPNVTHVINYDL-PTDIdDYVHRIGRTGRaGNTG----- 543
Cdd:COG1111 386 qaSKEGDKglTQKEQIEILERFRAGEFNVLVATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR-KREGrvvvl 463
|
170 180 190
....*....|....*....|....*....|....*...
gi 367037389 544 IA-----TAFFNRGNR------GIVRELIDLLKEANQE 570
Cdd:COG1111 464 IAkgtrdEAYYWSSRRkekkmkSILKKLKKLLDKQEKE 501
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
417-549 |
2.34e-16 |
|
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: 76.09 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 417 SENITQKIEYVEDIDKRSVLLD-ILHTHAGGLTLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNGK 495
Cdd:cd18794 1 RPNLFYSVRPKDKKDEKLDLLKrIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 367037389 496 CPILVATAVAARGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGIATAFF 549
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
175-404 |
3.09e-16 |
|
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: 78.52 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 175 VTPSGRDVPEPIL---TFSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVING--RDLMACAQTGSGKTGGFLFPILhqs 249
Cdd:cd18048 3 VEVLQRDPTSPLFsvkSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAML--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 250 ftqgpSPVPAqgggygrqRKAYPTALILAPTRELVSQ---IYDEARKFayrswvrpCVvygGADIGSQLR--QIERGCDL 324
Cdd:cd18048 80 -----SRVDA--------LKLYPQCLCLSPTFELALQtgkVVEEMGKF--------CV---GIQVIYAIRgnRPGKGTDI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 325 ----LVATPGRLVDLIERGR-ISLCNIKYLVLDEADRMLDM-GFEPQIRRIVQGedMPPTGqrQTLMFSATFPRDIQMLA 398
Cdd:cd18048 136 eaqiVIGTPGTVLDWCFKLRlIDVTNISVFVLDEADVMINVqGHSDHSVRVKRS--MPKEC--QMLLFSATFEDSVWAFA 211
|
....*.
gi 367037389 399 QDFLSD 404
Cdd:cd18048 212 ERIVPD 217
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
436-541 |
3.40e-16 |
|
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: 75.71 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 436 LLDILHTHAGGL----TLIFVETKRMADSLS---------------DFLINQNFPATSIHGDRTQRERERALELFRNGKC 496
Cdd:cd18802 12 LIEILREYFPKTpdfrGIIFVERRATAVVLSrllkehpstlafircGFLIGRGNSSQRKRSLMTQRKQKETLDKFRDGEL 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 367037389 497 PILVATAVAARGLDIPNVTHVINYDLPTDIDDYVHRIGRtGRAGN 541
Cdd:cd18802 92 NLLIATSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGR-ARAPN 135
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
224-389 |
8.52e-15 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 72.05 E-value: 8.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 224 GRDLMACAQTGSGKTGgFLFPILHQSFTQGPSPVpaqgggygrqrkayptaLILAPTRELVSQIYDEARKFAyrSWVRPC 303
Cdd:cd00046 1 GENVLITAPTGSGKTL-AALLAALLLLLKKGKKV-----------------LVLVPTKALALQTAERLRELF--GPGIRV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 304 -VVYGGADIGSQLRQIERGCDLLVATPGRLVDLIER-GRISLCNIKYLVLDEADRMLDMGFEPQIRRIVQGEDMPPTGQR 381
Cdd:cd00046 61 aVLVGGSSAEEREKNKLGDADIIIATPDMLLNLLLReDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQV 140
|
....*...
gi 367037389 382 qtLMFSAT 389
Cdd:cd00046 141 --ILLSAT 146
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
422-534 |
3.40e-13 |
|
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: 67.12 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 422 QKIEYVEDIdKRSVLLDILHT--HAGGLTLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNGKCP-- 497
Cdd:cd18793 3 PKIEEVVSG-KLEALLELLEElrEPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrv 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 367037389 498 ILVATAVAARGLDIPNVTHVINYDL---PTDID---DYVHRIG 534
Cdd:cd18793 82 FLLSTKAGGVGLNLTAANRVILYDPwwnPAVEEqaiDRAHRIG 124
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
211-540 |
1.49e-12 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 70.31 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 211 TPVQKYSIP-IVINGRDLMACAQTGSGKTggFL--FPILhQSFTQGPspvpaqgggygrqrkaypTALILAPTRELVSQI 287
Cdd:COG1204 24 YPPQAEALEaGLLEGKNLVVSAPTASGKT--LIaeLAIL-KALLNGG------------------KALYIVPLRALASEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 288 YDEARKFAYRSWVRPCVVYGGADIGSQLrqIERgCDLLVATPGRLvDLIERGRIS-LCNIKYLVLDEA------------ 354
Cdd:COG1204 83 YREFKRDFEELGIKVGVSTGDYDSDDEW--LGR-YDILVATPEKL-DSLLRNGPSwLRDVDLVVVDEAhliddesrgptl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 355 ----DRMLDMGFEPQIrrivqgedmpptgqrqtLMFSATF--PRDI-QML-AQDFLSDY--VFLSVGrVGSTSENITQKI 424
Cdd:COG1204 159 evllARLRRLNPEAQI-----------------VALSATIgnAEEIaEWLdAELVKSDWrpVPLNEG-VLYDGVLRFDDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 425 EYVEDIDKRSVLLDILHThaGGLTLIFVETKRMA-----------------------DSLSDFLIN------QNFP-ATS 474
Cdd:COG1204 221 SRRSKDPTLALALDLLEE--GGQVLVFVSSRRDAeslakkladelkrrltpeereelEELAEELLEvseethTNEKlADC 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 367037389 475 I-------HGDRTQRERERALELFRNGKCPILVATAVAARGLDIPnVTHVI------NYDLPTDIDDYVHRIGRTGRAG 540
Cdd:COG1204 299 LekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIirdtkrGGMVPIPVLEFKQMAGRAGRPG 376
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
423-540 |
7.40e-12 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 68.75 E-value: 7.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 423 KIEYVEDIdkrsvLLDILHTHAGGLTLIFVETKRMADSLSDFLINQNFPA------TSIHGDR--TQRERERALELFRNG 494
Cdd:PRK13766 348 KLEKLREI-----VKEQLGKNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAvrfvgqASKDGDKgmSQKEQIEILDKFRAG 422
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 367037389 495 KCPILVATAVAARGLDIPNVTHVINYD-LPTDIdDYVHRIGRTGRAG 540
Cdd:PRK13766 423 EFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGRQE 468
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
432-536 |
8.12e-12 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 68.33 E-value: 8.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 432 KRSVLLDILHTH--AGGLTLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNGK-CP-ILVATAVAAR 507
Cdd:COG0553 534 KLEALLELLEELlaEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPeAPvFLISLKAGGE 613
|
90 100 110
....*....|....*....|....*....|....*
gi 367037389 508 GLDIPNVTHVINYDL---PTDID---DYVHRIGRT 536
Cdd:COG0553 614 GLNLTAADHVIHYDLwwnPAVEEqaiDRAHRIGQT 648
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
188-404 |
4.01e-11 |
|
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both mRNA (mRNA) export from the nucleus into the cytoplasm and in mRNA translation. DDX19 functions in the nucleus in resolving RNA:DNA hybrids (R-loops). Activation of a DNA damage response pathway dependent upon the ATR kinase, a major regulator of replication fork progression, stimulates translocation of DDX19 from the cytoplasm into the nucleus. Only nuclear Ddx19 is competent to resolve R-loops. DDX19 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350805 [Multi-domain] Cd Length: 205 Bit Score: 62.82 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 188 TFSNPPLDPHLLSNIELARYKIPTPVQKYSIPIVING--RDLMACAQTGSGKTGGFLFPILHQSftqgpspVPAQgggyg 265
Cdd:cd18047 2 SFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEppQNLIAQSQSGTGKTAAFVLAMLSQV-------EPAN----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 266 rqrkAYPTALILAPTRELVSQ---IYDEARKFayrswvRPCVVYGGADIGSQLrqiERGC----DLLVATPGRLVD-LIE 337
Cdd:cd18047 70 ----KYPQCLCLSPTYELALQtgkVIEQMGKF------YPELKLAYAVRGNKL---ERGQkiseQIVIGTPGTVLDwCSK 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 367037389 338 RGRISLCNIKYLVLDEADRML-DMGFEPQIRRIvqgEDMPPTGQrQTLMFSATFPRDIQMLAQDFLSD 404
Cdd:cd18047 137 LKFIDPKKIKVFVLDEADVMIaTQGHQDQSIRI---QRMLPRNC-QMLLFSATFEDSVWKFAQKVVPD 200
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
498-543 |
3.83e-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: 53.48 E-value: 3.83e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 367037389 498 ILVATAVAARGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTG 543
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
480-538 |
8.87e-09 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 54.67 E-value: 8.87e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 480 TQRERERALELFRNGKCPILVATAVAARGLDIPNVTHVINYD-LPTDIdDYVHRIGRTGR 538
Cdd:cd18801 75 SQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDaSPSPI-RMIQRMGRTGR 133
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
448-518 |
2.12e-08 |
|
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: 52.56 E-value: 2.12e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 367037389 448 TLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERER-ALELFRNG--KCPILVATAVAARGLDIPNVTHVI 518
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGDeALILLFFGelKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
221-545 |
1.50e-07 |
|
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: 54.84 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 221 VINGRDLMACAQTGSGKTGGFLFPILhQSFTQGPSpvpaqgggygrqrkayPTALILAPTRELvsqIYDEARKF-----A 295
Cdd:COG1205 68 ARAGKNVVIATPTASGKSLAYLLPVL-EALLEDPG----------------ATALYLYPTKAL---ARDQLRRLrelaeA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 296 YRSWVRPCVVYGgaDIGSQLRQ-IERGCDLLVATPgrlvDLIERG------RIS--LCNIKYLVLDEA------------ 354
Cdd:COG1205 128 LGLGVRVATYDG--DTPPEERRwIREHPDIVLTNP----DMLHYGllphhtRWArfFRNLRYVVIDEAhtyrgvfgshva 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 355 ---DRML----DMGFEPQIrrivqgedmpptgqrqtLMFSATF--PRDiqmLAQDFLSDYVFLsVGRVGSTSenitQKIE 425
Cdd:COG1205 202 nvlRRLRricrHYGSDPQF-----------------ILASATIgnPAE---HAERLTGRPVTV-VDEDGSPR----GERT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 426 YV-------EDIDKRSVLL---DILHTHA-GGL-TLIFV----ETKRMADSLSDFLINQNFpATSI---HGDRTQREReR 486
Cdd:COG1205 257 FVlwnpplvDDGIRRSALAeaaRLLADLVrEGLrTLVFTrsrrGAELLARYARRALREPDL-ADRVaayRAGYLPEER-R 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 367037389 487 ALE-LFRNGKCPILVAT-AVAArGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGIA 545
Cdd:COG1205 335 EIErGLRSGELLGVVSTnALEL-GIDIGGLDAVVLAGYPGTRASFWQQAGRAGRRGQDSLV 394
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
426-544 |
2.08e-07 |
|
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: 51.15 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 426 YVEDIDKRSVLLDILHTHAGGlTLIFVET---KRMADSLSDFLINQNFPATSIHgdrtqRERERALELFRNGKCPILVAT 502
Cdd:cd18798 6 YIEDSDSLEKLLELVKKLGDG-GLIFVSIdygKEYAEELKEFLERHGIKAELAL-----SSTEKNLEKFEEGEIDVLIGV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 367037389 503 A----VAARGLDIPN-VTHVINYDLPtdIDDYVHRIGRTGRAGNTGI 544
Cdd:cd18798 80 AsyygVLVRGIDLPErIKYAIFYGVP--VTTYIQASGRTSRLYAGGL 124
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
423-549 |
3.60e-07 |
|
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex helicase XPB (xeroderma pigmentosum type B) subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350176 [Multi-domain] Cd Length: 153 Bit Score: 50.33 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 423 KIEYVEDIDKRsvlldilhtHAGG-LTLIFVETKRMADSLS-DFLInqnfPAtsIHGDRTQRERERALELFRNGKCPILV 500
Cdd:cd18789 35 KLRALEELLKR---------HEQGdKIIVFTDNVEALYRYAkRLLK----PF--ITGETPQSEREEILQNFREGEYNTLV 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 367037389 501 ATAVAARGLDIP--NVTHVINYDLPTDiDDYVHRIGRTGRAGNTGIATAFF 549
Cdd:cd18789 100 VSKVGDEGIDLPeaNVAIQISGHGGSR-RQEAQRLGRILRPKKGGGKNAFF 149
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
224-354 |
8.44e-07 |
|
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: 49.57 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 224 GRDLMACAQTGSGKTGGFLFPILHQSFTQGpspvpaqgggygrQRKAYptaliLAPTRELVSQIYDEARKFAYRSWVRPC 303
Cdd:cd17921 17 GDSVLVSAPTSSGKTLIAELAILRALATSG-------------GKAVY-----IAPTRALVNQKEADLRERFGPLGKNVG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 367037389 304 VVYGGADIGSQLrqiERGCDLLVATPGRLVDLIERGRISLC-NIKYLVLDEA 354
Cdd:cd17921 79 LLTGDPSVNKLL---LAEADILVATPEKLDLLLRNGGERLIqDVRLVVVDEA 127
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
436-541 |
1.27e-06 |
|
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: 48.41 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 436 LLDILHTHAGglTLIFVETKRMADSLSD---FLINQNFPATSI---HG--DRTQRER-ERALelfRNGKCPILVATAVAA 506
Cdd:cd18796 31 VIFLLERHKS--TLVFTNTRSQAERLAQrlrELCPDRVPPDFIalhHGslSRELREEvEAAL---KRGDLKVVVATSSLE 105
|
90 100 110
....*....|....*....|....*....|....*
gi 367037389 507 RGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGN 541
Cdd:cd18796 106 LGIDIGDVDLVIQIGSPKSVARLLQRLGRSGHRPG 140
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
210-396 |
4.49e-06 |
|
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase RecG family is part of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350676 [Multi-domain] Cd Length: 180 Bit Score: 47.41 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 210 PTPVQKYSIPIVING------RDLMACAQTGSGKTGGFLFPIlHQSFTQGPSpvpaqgggygrqrkayptALILAPTREL 283
Cdd:cd17918 16 LTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAA-LLAYKNGKQ------------------VAILVPTEIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 284 VSQIYDEARKFAyrSWVRPCVVYGGADigsqlRQIERGCDLLVATPGrlvdLIERGRISLcNIKYLVLDEADRMldmgfe 363
Cdd:cd17918 77 AHQHYEEARKFL--PFINVELVTGGTK-----AQILSGISLLVGTHA----LLHLDVKFK-NLDLVIVDEQHRF------ 138
|
170 180 190
....*....|....*....|....*....|....
gi 367037389 364 pqirRIVQGEDMPPTGQRQTLMFSAT-FPRDIQM 396
Cdd:cd17918 139 ----GVAQREALYNLGATHFLEATATpIPRTLAL 168
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
424-562 |
7.21e-06 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 49.33 E-value: 7.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 424 IEY--VEDIDKRSVLLDILHTHAGGLTLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNGKCPILVA 501
Cdd:PRK11057 213 IRYtlVEKFKPLDQLMRYVQEQRGKSGIIYCNSRAKVEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVA 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 367037389 502 TAVAARGLDIPNVTHVINYDLPTDIDDYVHRIGRTGRAGNTGIATAFFNRGNRGIVRELID 562
Cdd:PRK11057 293 TVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAGRDGLPAEAMLFYDPADMAWLRRCLE 353
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
475-521 |
7.83e-06 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 46.49 E-value: 7.83e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 367037389 475 IHGDRTQRERERALELFRNGKCPILVATAVAARGLDIPNVTHVINYD 521
Cdd:cd18792 66 LHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNANTMIIED 112
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
475-540 |
9.80e-06 |
|
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a critical role in recombination and DNA repair. RecG helps process Holliday junction intermediates to mature products by catalyzing branch migration. It is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350198 [Multi-domain] Cd Length: 159 Bit Score: 46.18 E-value: 9.80e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 367037389 475 IHGDRTQRERERALELFRNGKCPILVATAVAARGLDIPNVTHVINYD-----LPTdiddyVHRI-GRTGRAG 540
Cdd:cd18811 67 LHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIEDaerfgLSQ-----LHQLrGRVGRGD 133
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
448-521 |
1.34e-05 |
|
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) plays a central role in nucleotide excision repair (NER). Together with other components of the NER system, like UvrA, UvrC, UvrD (helicase II), and DNA polymerase I, it recognizes and cleaves damaged DNA in a multistep ATP-dependent reaction. UvrB is critical for the second phase of damage recognition by verifying the nature of the damage and forming the pre-incision complex. Its ATPase site becomes activated in the presence of UvrA and damaged DNA. Its activity is strand destabilization via distortion of the DNA at lesion site, with very limited DNA unwinding. UvrB is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350177 [Multi-domain] Cd Length: 171 Bit Score: 46.08 E-value: 1.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 367037389 448 TLIFVETKRMADSLSDFLINQNFPATSIHGDRTQRERERALELFRNGKCPILVATAVAARGLDIPNVTHVINYD 521
Cdd:cd18790 30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILD 103
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
205-261 |
3.54e-05 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 47.02 E-value: 3.54e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 367037389 205 ARYKIPTPVQKYSIPIVINGRDLMACAQTGSGKT-GGFLfPILHQSFTQGPSPVPAQG 261
Cdd:COG1201 20 ARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFL-PALDELARRPRPGELPDG 76
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
434-545 |
3.75e-05 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 44.47 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 434 SVLLDILHTHAGGL-TLIFVETKRMADSLSDFLINQNFpatsIHGDRTQRERERALELFRNGKCPILVATAVAARGLDIP 512
Cdd:cd18795 31 IIVLLKIETVSEGKpVLVFCSSRKECEKTAKDLAGIAF----HHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNLP 106
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 367037389 513 NVTHVIN----YDLPT----DIDDYVHRIGRTGRAG--NTGIA 545
Cdd:cd18795 107 ARTVIIKgtqrYDGKGyrelSPLEYLQMIGRAGRPGfdTRGEA 149
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
225-354 |
8.19e-05 |
|
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: 44.18 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 225 RDLMACAQTGSGKTggfLFPIL-----HQSFTQGPSPvpaqgggyGRQrkayptALILAPTRELVSQIYDearkfAYRSW 299
Cdd:cd18034 17 RNTIVVLPTGSGKT---LIAVMlikemGELNRKEKNP--------KKR------AVFLVPTVPLVAQQAE-----AIRSH 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 367037389 300 VRPCV--VYGGADIGSQLRQIERGC----DLLVATPGRLVDLIERGRISLCNIKYLVLDEA 354
Cdd:cd18034 75 TDLKVgeYSGEMGVDKWTKERWKEElekyDVLVMTAQILLDALRHGFLSLSDINLLIFDEC 135
|
|
| DEXHc_Hef |
cd18035 |
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs ... |
265-356 |
1.09e-04 |
|
DEXH-box helicase domain of Hef; Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. All archaea encode a protein of the XPF/MUS81/FANCM family of endonucleases. It exists in two forms: a long form, referred as Hef which consists of an N-terminal helicase fused to a C-terminal nuclease and is specific to euryarchaea and a short form, referred as XPF which lacks the helicase domain and is specific to crenarchaea and thaumarchaea. Hef has the unique feature of having both active helicase and nuclease domains. This domain configuration is highly similar with the human FANCM, a possible ortholog of archaeal Hef proteins. Hef is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350793 [Multi-domain] Cd Length: 181 Bit Score: 43.66 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 265 GRQRKAYPTALILAPTRELVSQIYDEARKFAyrSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRISLC 344
Cdd:cd18035 39 DRLTKKGGKVLILAPSRPLVEQHAENLKRVL--NIPDKITSLTGEVKPEERAERWDASKIIVATPQVIENDLLAGRITLD 116
|
90
....*....|..
gi 367037389 345 NIKYLVLDEADR 356
Cdd:cd18035 117 DVSLLIFDEAHH 128
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
226-540 |
1.29e-04 |
|
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an alignment of Cas3, a protein found in association with CRISPR repeat elements in a broad range of bacteria and archaea. Cas3 appears to be a helicase, with regions found by pfam00270 (DEAD/DEAH box helicase) and pfam00271 (Helicase conserved C-terminal domain). Some but not all members have an N-terminal HD domain region (pfam01966) that is not included within this model.
Pssm-ID: 273707 [Multi-domain] Cd Length: 359 Bit Score: 44.75 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 226 DLMACAQTGSGKT-GGFLF---PILHQSFTQGPSPVPAQ---GGGYGRQRKAYPTALILAPTRELVSQIYDEARKFAyrs 298
Cdd:TIGR01587 1 LLVIEAPTGYGKTeAALLWalhSIKSQKADRVIIALPTRatiNAMYRRAKELFGSELVGLHHSSSFSRIKEMGDSEE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 299 WVRPCVVYGGADIGSQLRQIErgcdllVATPGRLvdLIERGR------ISLCNIKY--LVLDEADRMLD--MGFEPQIRR 368
Cdd:TIGR01587 78 FEHLFPLYIHSNDKLFLDPIT------VCTIDQV--LKSVFGefghyeFTLASIANslLIFDEVHFYDEytLALILAVLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 369 IVQGEDMPptgqrqTLMFSATFPRDIQMLAQDFlsDYVFLSVGRVGSTSENITQ----KIEYVEDIDKRSVLLDILHTHA 444
Cdd:TIGR01587 150 VLKDNDVP------ILLMSATLPKFLKEYAEKI--GYVEFNEPLDLKEERRFENhrfiLIESDKVGEISSLERLLEFIKK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 445 GGLTLIFVETKRMADSLSDfLINQNFPATSI---HG-----DRTQRERERALELFRNGKCPILVATAVAARGLDIpNVTH 516
Cdd:TIGR01587 222 GGSIAIIVNTVDRAQEFYQ-QLKEKAPEEEIilyHSrftekDRAKKEAELLREMKKSNEKFVIVATQVIEASLDI-SADV 299
|
330 340
....*....|....*....|....
gi 367037389 517 VINYDLPtdIDDYVHRIGRTGRAG 540
Cdd:TIGR01587 300 MITELAP--IDSLIQRLGRLHRYG 321
|
|
| DEXHc_RIG-I |
cd17927 |
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I ... |
215-356 |
1.36e-04 |
|
DEXH-box helicase domain of DEAD-like helicase RIG-I family proteins; Members of the RIG-I family include FANCM, dicer, Hef, and the RIG-I-like receptors. Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). Hef (helicase-associated endonuclease fork-structure) is involved in stalled replication fork repair. RIG-I-like receptors (RLRs) sense cytoplasmic viral RNA and comprises RIG-I, RLR-2/MDA5 (melanoma differentiation-associated protein 5) and RLR-3/LGP2 (laboratory of genetics and physiology 2). The RIG-I family is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350685 [Multi-domain] Cd Length: 201 Bit Score: 43.58 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 215 KYSIPIV---INGRDLMACAQTGSGKTGGFLFpILHQSFTQGPSpvpaqgggyGRQRKayptALILAPTRELVSQIYDEA 291
Cdd:cd17927 5 NYQLELAqpaLKGKNTIICLPTGSGKTFVAVL-ICEHHLKKFPA---------GRKGK----VVFLANKVPLVEQQKEVF 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 367037389 292 RKFAYRSWVRPCVVYGGADIGSQLRQIERGCDLLVATPGRLVDLIERGRI-SLCNIKYLVLDEADR 356
Cdd:cd17927 71 RKHFERPGYKVTGLSGDTSENVSVEQIVESSDVIIVTPQILVNDLKSGTIvSLSDFSLLVFDECHN 136
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
223-354 |
3.06e-04 |
|
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: 42.19 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 223 NGRDLMACAQTGSGKTGGFLFPILHQSFtqgpspvpaqgggygrqRKAYPTALILAPTRELvsqIYDEARKFayRSWVRP 302
Cdd:cd17923 14 AGRSVVVTTGTASGKSLCYQLPILEALL-----------------RDPGSRALYLYPTKAL---AQDQLRSL--RELLEQ 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 367037389 303 CV------VYGG-ADIGSQLRQIERGCDLLVATPGRLVDLI----ERGRISLCNIKYLVLDEA 354
Cdd:cd17923 72 LGlgirvaTYDGdTPREERRAIIRNPPRILLTNPDMLHYALlphhDRWARFLRNLRYVVLDEA 134
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
206-238 |
3.41e-04 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 44.11 E-value: 3.41e-04
10 20 30
....*....|....*....|....*....|...
gi 367037389 206 RYKIPTPVQKYSIPIVINGRDLMACAQTGSGKT 238
Cdd:PRK13767 29 KFGTFTPPQRYAIPLIHEGKNVLISSPTGSGKT 61
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
479-543 |
4.09e-04 |
|
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication factor Y or primosomal protein N', is a 3'-->5' DNA helicase that acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. PriA is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350191 [Multi-domain] Cd Length: 238 Bit Score: 42.62 E-value: 4.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 367037389 479 RTQRERERALELFRNGKCPILVATAVAARGLDIPNVTHV--INYDLPTDIDDY---------VHRI-GRTGRAGNTG 543
Cdd:cd18804 128 RKKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVgiLNADSGLNSPDFraserafqlLTQVsGRAGRGDKPG 204
|
|
| SF2_C_TRCF |
cd18810 |
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair ... |
475-545 |
1.05e-03 |
|
C-terminal helicase domain of the transcription-repair coupling factor; Transcription-repair coupling factor (TrcF) dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. TrcF is a DEAD-like helicase belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350197 [Multi-domain] Cd Length: 151 Bit Score: 40.02 E-value: 1.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 367037389 475 IHGDRTQRERERALELFRNGKCPILVATAVAARGLDIPNV-THVINydlptDIDDY----VHRI-GRTGRAGNTGIA 545
Cdd:cd18810 57 AHGQMTENELEEVMLEFAKGEYDILVCTTIIESGIDIPNAnTIIIE-----RADKFglaqLYQLrGRVGRSKERAYA 128
|
|
| PriA |
COG1198 |
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ... |
479-515 |
3.24e-03 |
|
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440811 [Multi-domain] Cd Length: 728 Bit Score: 40.87 E-value: 3.24e-03
10 20 30
....*....|....*....|....*....|....*..
gi 367037389 479 RTQRERERALELFRNGKCPILVATAVAARGLDIPNVT 515
Cdd:COG1198 515 RRKGALEKLLEAFARGEADILVGTQMLAKGHDFPNVT 551
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
434-543 |
3.63e-03 |
|
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members 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: 350178 [Multi-domain] Cd Length: 171 Bit Score: 38.67 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 434 SVLLDILHTHAGGLTLIFV----ETKRMADSLSDFLINQNFPATSI---HGDRTQRERERALELFRNGKCPILVATAVAA 506
Cdd:cd18791 32 RLILQIHRTEEPGDILVFLpgqeEIERLCELLREELLSPDLGKLLVlplHSSLPPEEQQRVFEPPPPGVRKVVLATNIAE 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 367037389 507 RGLDIPNVTHVI--------NYDLPTDIDDYV-HRIG------RTGRAGNTG 543
Cdd:cd18791 112 TSITIPGVVYVIdsglvkekVYDPRTGLSSLVtVWISkasaeqRAGRAGRTR 163
|
|
| ComFA |
COG4098 |
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, ... |
449-518 |
3.73e-03 |
|
Superfamily II DNA/RNA helicase required for DNA uptake (late competence protein) [Replication, recombination and repair];
Pssm-ID: 443274 [Multi-domain] Cd Length: 451 Bit Score: 40.24 E-value: 3.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 367037389 449 LIFVETKRMADSLSDFLInQNFPATSIHG----DRtqrERERALELFRNGKCPILVATAVAARGLDIPNVtHVI 518
Cdd:COG4098 323 LIFVPTIELLEQLVALLQ-KLFPEERIAGvhaeDP---ERKEKVQAFRDGEIPILVTTTILERGVTFPNV-DVA 391
|
|
| DEXHc_Brr2_2 |
cd18021 |
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ... |
230-354 |
7.05e-03 |
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C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350779 [Multi-domain] Cd Length: 191 Bit Score: 38.39 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 367037389 230 CAQTGSGKTGGFLFPILHqSFTQGPspvpaqgggYGRqrkayptALILAPTRELVSQIYDE-ARKFAyRSWVRPCVVYGG 308
Cdd:cd18021 25 GAPTGSGKTVCAELALLR-HWRQNP---------KGR-------AVYIAPMQELVDARYKDwRAKFG-PLLGKKVVKLTG 86
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90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 367037389 309 aDIGSQLRQIERGcDLLVATPGRLvDLIER---GRISLCNIKYLVLDEA 354
Cdd:cd18021 87 -ETSTDLKLLAKS-DVILATPEQW-DVLSRrwkQRKNVQSVELFIADEL 132
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