|
Name |
Accession |
Description |
Interval |
E-value |
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
233-619 |
8.77e-158 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 462.31 E-value: 8.77e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 233 FSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDGPDAvhrsvtssggrk 312
Cdd:COG0513 4 FADLGLSPPLLKALAELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPRA------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 313 kqyPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCR 392
Cdd:COG0513 72 ---PQALILAPTRELALQVAEELRKLAKYLGLRVATVYGG-VSIGRQIRALKRGVDIVVATPGRLLDLIERGALDLSGVE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 393 YLVLDEADRMLDMGFEPQIRQIVEcnRMPskEERITAMFSATFPKEIQLLAQDFLKeNYVFLAVGRVGSTSENIMQKIVW 472
Cdd:COG0513 148 TLVLDEADRMLDMGFIEDIERILK--LLP--KERQTLLFSATMPPEIRKLAKRYLK-NPVRIEVAPENATAETIEQRYYL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 473 VEEDEKRSYLMDLLDATGDSSlTLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAVA 552
Cdd:COG0513 223 VDKRDKLELLRRLLRDEDPER-AIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVA 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226437753 553 ARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSFFNDKNRNIARELMDLIveaNQELP 619
Cdd:COG0513 302 ARGIDIDDVSHVINYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRLLRAIEKLI---GQKIE 365
|
|
| DEADc_DDX3_DDX4 |
cd17967 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX3 and DDX4; This subfamily includes ... |
233-460 |
1.27e-141 |
|
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: 413.04 E-value: 1.27e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 233 FSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDGPDAvhrsvtSSGGRK 312
Cdd:cd17967 2 FEEAGLRELLLENIKRAGYTKPTPVQKYAIPIILAGRDLMACAQTGSGKTAAFLLPIISKLLEDGPPS------VGRGRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 313 KQYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGRENYkDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCR 392
Cdd:cd17967 76 KAYPSALILAPTRELAIQIYEEARKFSYRSGVRSVVVYGGADVV-HQQLQLLRGCDILVATPGRLVDFIERGRISLSSIK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226437753 393 YLVLDEADRMLDMGFEPQIRQIVECNRMPSKEERITAMFSATFPKEIQLLAQDFLKeNYVFLAVGRVG 460
Cdd:cd17967 155 FLVLDEADRMLDMGFEPQIRKIVEHPDMPPKGERQTLMFSATFPREIQRLAADFLK-NYIFLTVGRVG 221
|
|
| DEADc_DDX3 |
cd18051 |
DEAD-box helicase domain of DEAD box protein 3; DDX3 (also called helicase-like protein, DEAD ... |
211-461 |
4.61e-141 |
|
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: 412.90 E-value: 4.61e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 211 FDKYEEIPVEATGDDVPQPISLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLV 290
Cdd:cd18051 1 FDKYEDIPVEATGENCPPHIETFSDLDLGEIIRNNIELARYTKPTPVQKHAIPIIKSKRDLMACAQTGSGKTAAFLLPIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 291 NAILQDGPDAVHRSVTSSGGRKKQYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGrENYKDQIHKLRLGCHIL 370
Cdd:cd18051 81 SQIYEQGPGESLPSESGYYGRRKQYPLALVLAPTRELASQIYDEARKFAYRSRVRPCVVYGG-ADIGQQMRDLERGCHLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 371 IATPGRLIDVMDQGLIGMEGCRYLVLDEADRMLDMGFEPQIRQIVECNRMPSKEERITAMFSATFPKEIQLLAQDFLkEN 450
Cdd:cd18051 160 VATPGRLVDMLERGKIGLDYCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPTGERQTLMFSATFPKEIQMLARDFL-DN 238
|
250
....*....|.
gi 226437753 451 YVFLAVGRVGS 461
Cdd:cd18051 239 YIFLAVGRVGS 249
|
|
| DEADc_DDX4 |
cd18052 |
DEAD-box helicase domain of DEAD box protein 4; DEAD box protein 4 (DDX4, also known as VASA ... |
198-460 |
3.90e-134 |
|
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: 395.87 E-value: 3.90e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 198 EQELFSGQLSGINFDKYEEIPVEATGDDVPQPISLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQT 277
Cdd:cd18052 10 EDEIFATIQTGINFDKYDEIPVEVTGRNPPPAILTFEEANLCETLLKNIRKAGYEKPTPVQKYAIPIILAGRDLMACAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 278 GSGKTAAFLVPLVNAILQDGpdavhrsVTSSGGRKKQYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGrENYK 357
Cdd:cd18052 90 GSGKTAAFLLPVLTGMMKEG-------LTASSFSEVQEPQALIVAPTRELANQIFLEARKFSYGTCIRPVVVYGG-VSVG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 358 DQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRMLDMGFEPQIRQIVECNRMPSKEERITAMFSATFPK 437
Cdd:cd18052 162 HQIRQIEKGCHILVATPGRLLDFIGRGKISLSKLKYLILDEADRMLDMGFGPEIRKLVSEPGMPSKEDRQTLMFSATFPE 241
|
250 260
....*....|....*....|...
gi 226437753 438 EIQLLAQDFLKENYVFLAVGRVG 460
Cdd:cd18052 242 EIQRLAAEFLKEDYLFLTVGRVG 264
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
127-626 |
9.58e-120 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 369.10 E-value: 9.58e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 127 DRGDGGSSNFSRGGYNNRDEGSDNRGSGR---SYNNDRRDNGGDG-QNTRWNNLDAPPsrgtskWENRGARDERIEQELF 202
Cdd:PTZ00110 31 SNPYGNYQANHQDNYGGFRPGYGNYSGGYggfGMNSYGSSTLGKRlQPIDWKSINLVP------FEKNFYKEHPEVSALS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 203 SGQLSGINfdKYEEIPVEAtGDDVPQPISLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKT 282
Cdd:PTZ00110 105 SKEVDEIR--KEKEITIIA-GENVPKPVVSFEYTSFPDYILKSLKNAGFTEPTPIQVQGWPIALSGRDMIGIAETGSGKT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 283 AAFLVPLVNAILqdgpdAVHRSvtssggRKKQYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGRENyKDQIHK 362
Cdd:PTZ00110 182 LAFLLPAIVHIN-----AQPLL------RYGDGPIVLVLAPTRELAEQIREQCNKFGASSKIRNTVAYGGVPK-RGQIYA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 363 LRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRMLDMGFEPQIRQIVECNRmpskEERITAMFSATFPKEIQLL 442
Cdd:PTZ00110 250 LRRGVEILIACPGRLIDFLESNVTNLRRVTYLVLDEADRMLDMGFEPQIRKIVSQIR----PDRQTLMWSATWPKEVQSL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 443 AQDFLKENYVFLAVGRVG-STSENIMQKIVWVEEDEKRSYLMDLLDATG-DSSLTLVFVETKRGASDLAYYLNRQNYEVV 520
Cdd:PTZ00110 326 ARDLCKEEPVHVNVGSLDlTACHNIKQEVFVVEEHEKRGKLKMLLQRIMrDGDKILIFVETKKGADFLTKELRLDGWPAL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 521 TIHGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSFFN-DK 599
Cdd:PTZ00110 406 CIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVHRIGRTGRAGAKGASYTFLTpDK 485
|
490 500
....*....|....*....|....*..
gi 226437753 600 NRnIARELMDLIVEANQELPDWLEGMS 626
Cdd:PTZ00110 486 YR-LARDLVKVLREAKQPVPPELEKLS 511
|
|
| PRK11776 |
PRK11776 |
ATP-dependent RNA helicase DbpA; Provisional |
233-599 |
2.64e-96 |
|
ATP-dependent RNA helicase DbpA; Provisional
Pssm-ID: 236977 [Multi-domain] Cd Length: 460 Bit Score: 305.19 E-value: 2.64e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 233 FSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAIlqdgpDAVHRSVtssggrk 312
Cdd:PRK11776 6 FSTLPLPPALLANLNELGYTEMTPIQAQSLPAILAGKDVIAQAKTGSGKTAAFGLGLLQKL-----DVKRFRV------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 313 kQypsALVLSPTRELSLQIFNESRKFAYRTPITSAL-LYGGrENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGC 391
Cdd:PRK11776 74 -Q---ALVLCPTRELADQVAKEIRRLARFIPNIKVLtLCGG-VPMGPQIDSLEHGAHIIVGTPGRILDHLRKGTLDLDAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 392 RYLVLDEADRMLDMGFEPQIRQIVEcnRMPskEERITAMFSATFPKEIQLLAQDFLKENyvfLAVgRVGSTSEN--IMQK 469
Cdd:PRK11776 149 NTLVLDEADRMLDMGFQDAIDAIIR--QAP--ARRQTLLFSATYPEGIAAISQRFQRDP---VEV-KVESTHDLpaIEQR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 470 IVWVEEDEKRSYLMDLLDATGDSSlTLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVAT 549
Cdd:PRK11776 221 FYEVSPDERLPALQRLLLHHQPES-CVVFCNTKKECQEVADALNAQGFSALALHGDLEQRDRDQVLVRFANRSCSVLVAT 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 226437753 550 AVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSFFNDK 599
Cdd:PRK11776 300 DVAARGLDIKALEAVINYELARDPEVHVHRIGRTGRAGSKGLALSLVAPE 349
|
|
| PRK04837 |
PRK04837 |
ATP-dependent RNA helicase RhlB; Provisional |
233-595 |
3.17e-88 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235314 [Multi-domain] Cd Length: 423 Bit Score: 283.02 E-value: 3.17e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 233 FSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILqdgpdavhrSVTSSGGRK 312
Cdd:PRK04837 10 FSDFALHPQVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTATFHYLL---------SHPAPEDRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 313 KQYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCR 392
Cdd:PRK04837 81 VNQPRALIMAPTRELAVQIHADAEPLAQATGLKLGLAYGG-DGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 393 YLVLDEADRMLDMGFEPQIRQIVecNRMPSKEERITAMFSATFPKEIQLLAQDFLKE-NYVFLAVGRvgSTSENIMQKIV 471
Cdd:PRK04837 160 VVVLDEADRMFDLGFIKDIRWLF--RRMPPANQRLNMLFSATLSYRVRELAFEHMNNpEYVEVEPEQ--KTGHRIKEELF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 472 WVEEDEKrsylMDLLdatgdssLTL----------VFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTG 541
Cdd:PRK04837 236 YPSNEEK----MRLL-------QTLieeewpdraiIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILEEFTRG 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 226437753 542 TAPILVATAVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSF 595
Cdd:PRK04837 305 DLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISL 358
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
176-619 |
4.81e-88 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 285.53 E-value: 4.81e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 176 LDAPPSRGTSKWENRGARDER--IEQELFSGQLSGINFDKY-EEIPVEATGDDVPQPISLFSDLSLHEWIEENIKTAGYD 252
Cdd:PLN00206 63 AKSRVAVGAPKPKRLPATDECfyVRDPGSTSGLSSSQAELLrRKLEIHVKGEAVPPPILSFSSCGLPPKLLLNLETAGYE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 253 RPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAIlqdgpdAVHRSVTSSGGRKkqyPSALVLSPTRELSLQIF 332
Cdd:PLN00206 143 FPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPIISRC------CTIRSGHPSEQRN---PLAMVLTPTRELCVQVE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 333 NESRKFAYRTPITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRMLDMGFEPQIR 412
Cdd:PLN00206 214 DQAKVLGKGLPFKTALVVGG-DAMPQQLYRIQQGVELIVGTPGRLIDLLSKHDIELDNVSVLVLDEVDCMLERGFRDQVM 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 413 QIVECNRMPSkeeriTAMFSATFPKEIQLLAQDFLKeNYVFLAVGRVGSTSENIMQKIVWVEEDEKRSYLMDLLDATGD- 491
Cdd:PLN00206 293 QIFQALSQPQ-----VLLFSATVSPEVEKFASSLAK-DIILISIGNPNRPNKAVKQLAIWVETKQKKQKLFDILKSKQHf 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 492 SSLTLVFVETKRGASDLAYYLNR-QNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIPNVKHVINYDLP 570
Cdd:PLN00206 367 KPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMP 446
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 226437753 571 SDVDEYVHRIGRTGRVGNVGLATSFFNDKNRNIARELMDLIVEANQELP 619
Cdd:PLN00206 447 NTIKEYIHQIGRASRMGEKGTAIVFVNEEDRNLFPELVALLKSSGAAIP 495
|
|
| PRK04537 |
PRK04537 |
ATP-dependent RNA helicase RhlB; Provisional |
233-619 |
6.08e-84 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 235307 [Multi-domain] Cd Length: 572 Bit Score: 276.45 E-value: 6.08e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 233 FSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILqdgpdavhrSVTSSGGRK 312
Cdd:PRK04537 11 FSSFDLHPALLAGLESAGFTRCTPIQALTLPVALPGGDVAGQAQTGTGKTLAFLVAVMNRLL---------SRPALADRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 313 KQYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGREnYKDQIHKLRLGCHILIATPGRLIDVMDQ-GLIGMEGC 391
Cdd:PRK04537 82 PEDPRALILAPTRELAIQIHKDAVKFGADLGLRFALVYGGVD-YDKQRELLQQGVDVIIATPGRLIDYVKQhKVVSLHAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 392 RYLVLDEADRMLDMGFEPQIRQIVEcnRMPSKEERITAMFSATFPKEIQLLAQDFLKENYVfLAVGRVGSTSENIMQKIV 471
Cdd:PRK04537 161 EICVLDEADRMFDLGFIKDIRFLLR--RMPERGTRQTLLFSATLSHRVLELAYEHMNEPEK-LVVETETITAARVRQRIY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 472 WVEEDEKRSYLMDLLDATgDSSLTLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAV 551
Cdd:PRK04537 238 FPADEEKQTLLLGLLSRS-EGARTMVFVNTKAFVERVARTLERHGYRVGVLSGDVPQKKRESLLNRFQKGQLEILVATDV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226437753 552 AARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSFFNDKnrnIARELMDLIVEANQELP 619
Cdd:PRK04537 317 AARGLHIDGVKYVYNYDLPFDAEDYVHRIGRTARLGEEGDAISFACER---YAMSLPDIEAYIEQKIP 381
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
242-449 |
9.38e-83 |
|
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: 260.45 E-value: 9.38e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 242 IEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDGPdavhrsvtssggRKKQYPSALVL 321
Cdd:cd00268 1 LLKALKKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPK------------KKGRGPQALVL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 322 SPTRELSLQIFNESRKFAYRTPITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADR 401
Cdd:cd00268 69 APTRELAMQIAEVARKLGKGTGLKVAAIYGG-APIKKQIEALKKGPDIVVGTPGRLLDLIERGKLDLSNVKYLVLDEADR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 226437753 402 MLDMGFEPQIRQIVecNRMPSKeeRITAMFSATFPKEIQLLAQDFLKE 449
Cdd:cd00268 148 MLDMGFEEDVEKIL--SALPKD--RQTLLFSATLPEEVKELAKKFLKN 191
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
233-594 |
5.98e-81 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 264.75 E-value: 5.98e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 233 FSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDGPDAvhrsvtssggrK 312
Cdd:PRK10590 3 FDSLGLSPDILRAVAEQGYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHLITRQPHA-----------K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 313 KQYP-SALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGC 391
Cdd:PRK10590 72 GRRPvRALILTPTRELAAQIGENVRDYSKYLNIRSLVVFGG-VSINPQMMKLRGGVDVLVATPGRLLDLEHQNAVKLDQV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 392 RYLVLDEADRMLDMGFEPQIRQIVecNRMPSKeeRITAMFSATFPKEIQLLAQDFLKeNYVFLAVGRVGSTSENIMQKIV 471
Cdd:PRK10590 151 EILVLDEADRMLDMGFIHDIRRVL--AKLPAK--RQNLLFSATFSDDIKALAEKLLH-NPLEIEVARRNTASEQVTQHVH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 472 WVEEDEKRSYLMDLLdATGDSSLTLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAV 551
Cdd:PRK10590 226 FVDKKRKRELLSQMI-GKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDI 304
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 226437753 552 AARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATS 594
Cdd:PRK10590 305 AARGLDIEELPHVVNYELPNVPEDYVHRIGRTGRAAATGEALS 347
|
|
| PRK11192 |
PRK11192 |
ATP-dependent RNA helicase SrmB; Provisional |
233-595 |
2.67e-76 |
|
ATP-dependent RNA helicase SrmB; Provisional
Pssm-ID: 236877 [Multi-domain] Cd Length: 434 Bit Score: 251.79 E-value: 2.67e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 233 FSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPlvnAI--LQDGPdavhrsvtssgg 310
Cdd:PRK11192 3 FSELELDESLLEALQDKGYTRPTAIQAEAIPPALDGRDVLGSAPTGTGKTAAFLLP---ALqhLLDFP------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 311 RKKQ-YPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGReNYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGME 389
Cdd:PRK11192 68 RRKSgPPRILILTPTRELAMQVADQARELAKHTHLDIATITGGV-AYMNHAEVFSENQDIVVATPGRLLQYIKEENFDCR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 390 GCRYLVLDEADRMLDMGFEPQIRQIvecnrmpSKEER---ITAMFSATFPKE-IQLLAQDFLKENyVFLAVGrvGSTSE- 464
Cdd:PRK11192 147 AVETLILDEADRMLDMGFAQDIETI-------AAETRwrkQTLLFSATLEGDaVQDFAERLLNDP-VEVEAE--PSRREr 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 465 -NIMQkivWV----EEDEKRSYLMDLLdATGDSSLTLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFR 539
Cdd:PRK11192 217 kKIHQ---WYyradDLEHKTALLCHLL-KQPEVTRSIVFVRTRERVHELAGWLRKAGINCCYLEGEMVQAKRNEAIKRLT 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 226437753 540 TGTAPILVATAVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSF 595
Cdd:PRK11192 293 DGRVNVLVATDVAARGIDIDDVSHVINFDMPRSADTYLHRIGRTGRAGRKGTAISL 348
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
213-595 |
6.47e-76 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 252.14 E-value: 6.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 213 KYEEIPVEatgddvPQPI-SLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVN 291
Cdd:PRK01297 74 KLEDFVVE------PQEGkTRFHDFNLAPELMHAIHDLGFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIIN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 292 AILQDGPdavhrsvtssggRKKQY---PSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGREnYKDQIHKLRLG-C 367
Cdd:PRK01297 148 QLLQTPP------------PKERYmgePRALIIAPTRELVVQIAKDAAALTKYTGLNVMTFVGGMD-FDKQLKQLEARfC 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 368 HILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRMLDMGFEPQIRQIVEcnRMPSKEERITAMFSATFPKEIQLLAQDFL 447
Cdd:PRK01297 215 DILVATPGRLLDFNQRGEVHLDMVEVMVLDEADRMLDMGFIPQVRQIIR--QTPRKEERQTLLFSATFTDDVMNLAKQWT 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 448 KENyVFLAVGRVGSTSENIMQKIVWVEEDEKRSYLMDLLDATGDSSLtLVFVETKRGASDLAYYLNRQNYEVVTIHGDLK 527
Cdd:PRK01297 293 TDP-AIVEIEPENVASDTVEQHVYAVAGSDKYKLLYNLVTQNPWERV-MVFANRKDEVRRIEERLVKDGINAAQLSGDVP 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226437753 528 QFEREKHLDLFRTGTAPILVATAVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSF 595
Cdd:PRK01297 371 QHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINFTLPEDPDDYVHRIGRTGRAGASGVSISF 438
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
233-620 |
1.13e-70 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 242.45 E-value: 1.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 233 FSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAIlqdgpDAVHRSvtssggrk 312
Cdd:PRK11634 8 FADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLHNL-----DPELKA-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 313 kqyPSALVLSPTRELSLQIFNESRKFAYRTP-ITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGC 391
Cdd:PRK11634 75 ---PQILVLAPTRELAVQVAEAMTDFSKHMRgVNVVALYGG-QRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 392 RYLVLDEADRMLDMGFEPQIRQIVEcnRMPskEERITAMFSATFPKEIQLLAQDFLKENYVFLAVGRVgSTSENIMQKIV 471
Cdd:PRK11634 151 SGLVLDEADEMLRMGFIEDVETIMA--QIP--EGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSV-TTRPDISQSYW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 472 WVEEDEKRSYLMDLLDATgDSSLTLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAV 551
Cdd:PRK11634 226 TVWGMRKNEALVRFLEAE-DFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDV 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226437753 552 AARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSFFNDKNR----NIARELMDLIVEAnqELPD 620
Cdd:PRK11634 305 AARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERrllrNIERTMKLTIPEV--ELPN 375
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
242-449 |
7.45e-66 |
|
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: 216.08 E-value: 7.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 242 IEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPlvnAIlqdgpdaVHRSVTSSGGRKKQyPSALVL 321
Cdd:cd17966 1 VMDELKRQGFTEPTAIQAQGWPMALSGRDMVGIAQTGSGKTLAFLLP---AI-------VHINAQPPLERGDG-PIVLVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 322 SPTRELSLQIFNESRKFAYRTPITSALLYGGRENYKdQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADR 401
Cdd:cd17966 70 APTRELAQQIQQEANKFGGSSRLRNTCVYGGAPKGP-QIRDLRRGVEICIATPGRLIDFLDQGKTNLRRVTYLVLDEADR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 226437753 402 MLDMGFEPQIRQIVECNRmpskEERITAMFSATFPKEIQLLAQDFLKE 449
Cdd:cd17966 149 MLDMGFEPQIRKIVDQIR----PDRQTLMWSATWPKEVRRLAEDFLKD 192
|
|
| DEADc_DDX23 |
cd17945 |
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and ... |
246-449 |
2.74e-63 |
|
DEAD-box helicase domain of DEAD box protein 23; DDX23 (also called U5 snRNP 100kD protein and PRP28 homolog) is involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Diseases associated with DDX23 include distal hereditary motor neuropathy, type II. DDX23 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350703 [Multi-domain] Cd Length: 220 Bit Score: 209.87 E-value: 2.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 246 IKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDGPdavhrsVTSSggRKKQYPSALVLSPTR 325
Cdd:cd17945 5 IRKLGYKEPTPIQRQAIPIGLQNRDIIGIAETGSGKTAAFLIPLLVYISRLPP------LDEE--TKDDGPYALILAPTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 326 ELSLQIFNESRKFAYRTPITSALLYGGReNYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRMLDM 405
Cdd:cd17945 77 ELAQQIEEETQKFAKPLGIRVVSIVGGH-SIEEQAFSLRNGCEILIATPGRLLDCLERRLLVLNQCTYVVLDEADRMIDM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226437753 406 GFEPQIRQIVEcnRMPS------------------KEERITAMFSATFPKEIQLLAQDFLKE 449
Cdd:cd17945 156 GFEPQVTKILD--AMPVsnkkpdteeaeklaasgkHRYRQTMMFTATMPPAVEKIAKGYLRR 215
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
221-448 |
2.04e-61 |
|
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: 204.92 E-value: 2.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 221 ATGDDVPQPISLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQdgpda 300
Cdd:cd17953 2 VRGKDCPKPIQKWSQCGLSEKVLDLIKKLGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMFRHIKD----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 301 vHRSVTSSGGrkkqyPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDV 380
Cdd:cd17953 77 -QRPVKPGEG-----PIGLIMAPTRELALQIYVECKKFSKALGLRVVCVYGG-SGISEQIAELKRGAEIVVCTPGRMIDI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226437753 381 M---DQGLIGMEGCRYLVLDEADRMLDMGFEPQIRQIVEcNRMPSKEeriTAMFSATFPKEIQLLAQDFLK 448
Cdd:cd17953 150 LtanNGRVTNLRRVTYVVLDEADRMFDMGFEPQIMKIVN-NIRPDRQ---TVLFSATFPRKVEALARKVLH 216
|
|
| DEADc_MSS116 |
cd17964 |
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ... |
246-454 |
4.07e-60 |
|
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: 200.89 E-value: 4.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 246 IKTAGYDRPTPVQKYSI-PALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDGPDAVHRSVtssggrkkqypSALVLSPT 324
Cdd:cd17964 9 LTRMGFETMTPVQQKTLkPILSTGDDVLARAKTGTGKTLAFLLPAIQSLLNTKPAGRRSGV-----------SALIISPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 325 RELSLQIFNESRKF-AYRTPITSALLYGGRENYKDQIHKLRLGCHILIATPGRLIDVM-DQGLIGM-EGCRYLVLDEADR 401
Cdd:cd17964 78 RELALQIAAEAKKLlQGLRKLRVQSAVGGTSRRAELNRLRRGRPDILVATPGRLIDHLeNPGVAKAfTDLDYLVLDEADR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 226437753 402 MLDMGFEPQIRQIVECNRMPSKEERITAMFSATFPKEIQLLAQDFLKENYVFL 454
Cdd:cd17964 158 LLDMGFRPDLEQILRHLPEKNADPRQTLLFSATVPDEVQQIARLTLKKDYKFI 210
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
219-622 |
1.47e-59 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 206.22 E-value: 1.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 219 VEATGDDVpqpISLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVplvnAILQdgp 298
Cdd:PTZ00424 19 IESNYDEI---VDSFDALKLNEDLLRGIYSYGFEKPSAIQQRGIKPILDGYDTIGQAQSGTGKTATFVI----AALQ--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 299 dAVHRSVTSSggrkkqypSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGrENYKDQIHKLRLGCHILIATPGRLI 378
Cdd:PTZ00424 89 -LIDYDLNAC--------QALILAPTRELAQQIQKVVLALGDYLKVRCHACVGG-TVVRDDINKLKAGVHMVVGTPGRVY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 379 DVMDQGLIGMEGCRYLVLDEADRMLDMGFEPQIRQIVEcnRMPSKEEriTAMFSATFPKEIQLLAQDFLKENYVFLaVGR 458
Cdd:PTZ00424 159 DMIDKRHLRVDDLKLFILDEADEMLSRGFKGQIYDVFK--KLPPDVQ--VALFSATMPNEILELTTKFMRDPKRIL-VKK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 459 VGSTSENIMQKIVWVEEDE-KRSYLMDLLDatgdsSLTLV----FVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREK 533
Cdd:PTZ00424 234 DELTLEGIRQFYVAVEKEEwKFDTLCDLYE-----TLTITqaiiYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 534 HLDLFRTGTAPILVATAVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSFFNDKN----RNIARELMD 609
Cdd:PTZ00424 309 IMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASPENYIHRIGRSGRFGRKGVAINFVTPDDieqlKEIERHYNT 388
|
410
....*....|...
gi 226437753 610 LIVEANQELPDWL 622
Cdd:PTZ00424 389 QIEEMPMEVADYL 401
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
466-596 |
1.52e-58 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 193.88 E-value: 1.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 466 IMQKIVWVEEDEKRSYLMDLLDATGDSSLTLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPI 545
Cdd:cd18787 1 IKQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 226437753 546 LVATAVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSFF 596
Cdd:cd18787 81 LVATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEADc_DDX42 |
cd17952 |
DEAD-box helicase domain of DEAD box protein 42; DDX42 (also called Splicing Factor ... |
246-447 |
1.90e-57 |
|
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: 193.40 E-value: 1.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 246 IKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILqDGPDAVhrsvtssggrKKQYPSALVLSPTR 325
Cdd:cd17952 5 IRKQEYEQPTPIQAQALPVALSGRDMIGIAKTGSGKTAAFIWPMLVHIM-DQRELE----------KGEGPIAVIVAPTR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 326 ELSLQIFNESRKFAYRTPITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRMLDM 405
Cdd:cd17952 74 ELAQQIYLEAKKFGKAYNLRVVAVYGG-GSKWEQAKALQEGAEIVVATPGRLIDMVKKKATNLQRVTYLVLDEADRMFDM 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 226437753 406 GFEPQIRQIVECNRmpskEERITAMFSATFPKEIQLLAQDFL 447
Cdd:cd17952 153 GFEYQVRSIVGHVR----PDRQTLLFSATFKKKIEQLARDIL 190
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
244-457 |
4.76e-56 |
|
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: 189.72 E-value: 4.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 244 ENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDgpdavhrsvtssggRKKQYPSALVLSP 323
Cdd:cd17957 3 NNLEESGYREPTPIQMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKP--------------RKKKGLRALILAP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 324 TRELSLQIFNESRKFAYRTPITSALLYGGRENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRML 403
Cdd:cd17957 69 TRELASQIYRELLKLSKGTGLRIVLLSKSLEAKAKDGPKSITKYDILVSTPLRLVFLLKQGPIDLSSVEYLVLDEADKLF 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 226437753 404 DMGFEPQIRQIVE-CNrmpSKEERiTAMFSATFPKEIQLLAQDFLKeNYVFLAVG 457
Cdd:cd17957 149 EPGFREQTDEILAaCT---NPNLQ-RSLFSATIPSEVEELARSVMK-DPIRIIVG 198
|
|
| DEADc_DDX5 |
cd18049 |
DEAD-box helicase domain of DEAD box protein 5; DDX5 (also called RNA helicase P68, HLR1, ... |
210-457 |
9.50e-53 |
|
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: 182.13 E-value: 9.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 210 NFDKYEEIPVEatGDDVPQPISLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPL 289
Cdd:cd18049 5 QYRRSKEITVR--GHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 290 VNAIlqdgpdaVHRSVTSSGgrkkQYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGRENyKDQIHKLRLGCHI 369
Cdd:cd18049 83 IVHI-------NHQPFLERG----DGPICLVLAPTRELAQQVQQVAAEYGRACRLKSTCIYGGAPK-GPQIRDLERGVEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 370 LIATPGRLIDVMDQGLIGMEGCRYLVLDEADRMLDMGFEPQIRQIVECNRmpskEERITAMFSATFPKEIQLLAQDFLKE 449
Cdd:cd18049 151 CIATPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR----PDRQTLMWSATWPKEVRQLAEDFLKD 226
|
....*...
gi 226437753 450 nYVFLAVG 457
Cdd:cd18049 227 -YIHINIG 233
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
255-442 |
3.96e-52 |
|
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: 177.82 E-value: 3.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 255 TPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAIlqdgpdavhrsvtssgGRKKQYPSALVLSPTRELSLQIFNE 334
Cdd:pfam00270 1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAL----------------DKLDNGPQALVLAPTRELAEQIYEE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 335 SRKFAYRTPITSALLYGGrENYKDQIHKLRlGCHILIATPGRLIDVMDQgLIGMEGCRYLVLDEADRMLDMGFEPQIRQI 414
Cdd:pfam00270 65 LKKLGKGLGLKVASLLGG-DSRKEQLEKLK-GPDILVGTPGRLLDLLQE-RKLLKNLKLLVLDEAHRLLDMGFGPDLEEI 141
|
170 180
....*....|....*....|....*...
gi 226437753 415 VEcnRMPskEERITAMFSATFPKEIQLL 442
Cdd:pfam00270 142 LR--RLP--KKRQILLLSATLPRNLEDL 165
|
|
| DEADc_DDX27 |
cd17947 |
DEAD-box helicase domain of DEAD box protein 27; DDX27 (also called RHLP, deficiency of ... |
246-443 |
4.00e-52 |
|
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: 178.99 E-value: 4.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 246 IKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLvnailqdgpdaVHRSVTSSggRKKQYPSALVLSPTR 325
Cdd:cd17947 5 LSSLGFTKPTPIQAAAIPLALLGKDICASAVTGSGKTAAFLLPI-----------LERLLYRP--KKKAATRVLVLVPTR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 326 ELSLQIFNESRKFAYRTPITSALLYGGReNYKDQIHKLRLGCHILIATPGRLIDVMDQGL-IGMEGCRYLVLDEADRMLD 404
Cdd:cd17947 72 ELAMQCFSVLQQLAQFTDITFALAVGGL-SLKAQEAALRARPDIVIATPGRLIDHLRNSPsFDLDSIEILVLDEADRMLE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 226437753 405 MGFEPQIRQIVE-CNRmpskeERITAMFSATFPKEIQLLA 443
Cdd:cd17947 151 EGFADELKEILRlCPR-----TRQTMLFSATMTDEVKDLA 185
|
|
| DEADc_DDX43_DDX53 |
cd17958 |
DEAD-box helicase domain of DEAD box proteins 43 and 53; DDX43 (also called cancer/testis ... |
242-449 |
5.82e-52 |
|
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: 178.43 E-value: 5.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 242 IEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVP-LVNAILQDGPDAvhrsvtssggrKKQYPSALV 320
Cdd:cd17958 1 IMKEIKKQGFEKPSPIQSQAWPIILQGIDLIGVAQTGTGKTLAYLLPgFIHLDLQPIPRE-----------QRNGPGVLV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 321 LSPTRELSLQIFNESRKFAYRTpITSALLYGGReNYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEAD 400
Cdd:cd17958 70 LTPTRELALQIEAECSKYSYKG-LKSVCVYGGG-NRNEQIEDLSKGVDIIIATPGRLNDLQMNNVINLKSITYLVLDEAD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 226437753 401 RMLDMGFEPQIRQIVecnrMPSKEERITAMFSATFPKEIQLLAQDFLKE 449
Cdd:cd17958 148 RMLDMGFEPQIRKIL----LDIRPDRQTIMTSATWPDGVRRLAQSYLKD 192
|
|
| DEADc_DDX49 |
cd17955 |
DEAD-box helicase domain of DEAD box protein 49; DDX49 (also called Dbp8) is a member of the ... |
233-454 |
3.04e-49 |
|
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: 171.25 E-value: 3.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 233 FSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDgPDAVHrsvtssggrk 312
Cdd:cd17955 1 FEDLGLSSWLVKQCASLGIKEPTPIQKLCIPEILAGRDVIGGAKTGSGKTAAFALPILQRLSED-PYGIF---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 313 kqypsALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGRENYKdQIHKLRLGCHILIATPGRLIDVM---DQGLIGME 389
Cdd:cd17955 70 -----ALVLTPTRELAYQIAEQFRALGAPLGLRCCVIVGGMDMVK-QALELSKRPHIVVATPGRLADHLrssDDTTKVLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226437753 390 GCRYLVLDEADRMLDMGFEPQIRQIVECnrMPSKeeRITAMFSATFPKEIQLLAQDFLKENYVFL 454
Cdd:cd17955 144 RVKFLVLDEADRLLTGSFEDDLATILSA--LPPK--RQTLLFSATLTDALKALKELFGNKPFFWE 204
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
213-457 |
4.59e-49 |
|
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: 173.27 E-value: 4.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 213 KYEEIPVEatGDDVPQPISLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNA 292
Cdd:cd18050 46 RKKEITIR--GVGCPKPVFAFHQANFPQYVMDVLLDQNFKEPTPIQCQGFPLALSGRDMVGIAQTGSGKTLAYLLPAIVH 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 293 IlqdgpdaVHRSVTSSGgrkkQYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGRENyKDQIHKLRLGCHILIA 372
Cdd:cd18050 124 I-------NHQPYLERG----DGPICLVLAPTRELAQQVQQVADDYGKSSRLKSTCIYGGAPK-GPQIRDLERGVEICIA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 373 TPGRLIDVMDQGLIGMEGCRYLVLDEADRMLDMGFEPQIRQIVECNRmpskEERITAMFSATFPKEIQLLAQDFLKEnYV 452
Cdd:cd18050 192 TPGRLIDFLEAGKTNLRRCTYLVLDEADRMLDMGFEPQIRKIVDQIR----PDRQTLMWSATWPKEVRQLAEDFLRD-YV 266
|
....*
gi 226437753 453 FLAVG 457
Cdd:cd18050 267 QINIG 271
|
|
| DEADc_DDX55 |
cd17960 |
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ... |
246-447 |
1.20e-48 |
|
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: 169.68 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 246 IKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQdgpdavhrsvtSSGGRKKQYPSALVLSPTR 325
Cdd:cd17960 5 VAELGFTSMTPVQAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILLK-----------RKANLKKGQVGALIISPTR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 326 ELSLQIFNESRKFA--YRTPITSALLYGGRENYKDQIHKLRLGCHILIATPGRLID--VMDQGLIGMEGCRYLVLDEADR 401
Cdd:cd17960 74 ELATQIYEVLQSFLehHLPKLKCQLLIGGTNVEEDVKKFKRNGPNILVGTPGRLEEllSRKADKVKVKSLEVLVLDEADR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 226437753 402 MLDMGFEPQIRQIVECnrMPsKEERiTAMFSATFPKEIQLLAQDFL 447
Cdd:cd17960 154 LLDLGFEADLNRILSK--LP-KQRR-TGLFSATQTDAVEELIKAGL 195
|
|
| DEADc_DDX31 |
cd17949 |
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ... |
250-454 |
7.13e-48 |
|
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: 168.15 E-value: 7.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 250 GYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDGPDaVHRsvtSSGgrkkqyPSALVLSPTRELSL 329
Cdd:cd17949 10 GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLLSLEPR-VDR---SDG------TLALVLVPTRELAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 330 QIFNESRKFAYRTP-ITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDVMD--QGLiGMEGCRYLVLDEADRMLDMG 406
Cdd:cd17949 80 QIYEVLEKLLKPFHwIVPGYLIGG-EKRKSEKARLRKGVNILIATPGRLLDHLKntQSF-DVSNLRWLVLDEADRLLDMG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 226437753 407 FEPQIRQIVE---------CNRMPSKEERITAMFSATFPKEIQLLAqDFLKENYVFL 454
Cdd:cd17949 158 FEKDITKILEllddkrskaGGEKSKPSRRQTVLVSATLTDGVKRLA-GLSLKDPVYI 213
|
|
| DEADc_DDX54 |
cd17959 |
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ... |
233-449 |
1.58e-47 |
|
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: 166.71 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 233 FSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAIlqdgpdavHRSVTSSGGRk 312
Cdd:cd17959 3 FQSMGLSPPLLRAIKKKGYKVPTPIQRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKL--------KAHSPTVGAR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 313 kqypsALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCR 392
Cdd:cd17959 74 -----ALILSPTRELALQTLKVTKELGKFTDLRTALLVGG-DSLEEQFEALASNPDIIIATPGRLLHLLVEMNLKLSSVE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 226437753 393 YLVLDEADRMLDMGFEPQIRQIVEcnRMPskEERITAMFSATFPKEIQLLAQDFLKE 449
Cdd:cd17959 148 YVVFDEADRLFEMGFAEQLHEILS--RLP--ENRQTLLFSATLPKLLVEFAKAGLNE 200
|
|
| DEADc_DDX47 |
cd17954 |
DEAD-box helicase domain of DEAD box protein 47; DDX47 (also called E4-DEAD box protein) can ... |
233-442 |
3.07e-46 |
|
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: 163.26 E-value: 3.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 233 FSDLSLHEWIEENIKTAGYDRPTPVQKYSIP-ALQGgRDLMSCAQTGSGKTAAFLVPLVNAILQDgpdavhrsvtssggr 311
Cdd:cd17954 2 FKELGVCEELCEACEKLGWKKPTKIQEEAIPvALQG-RDIIGLAETGSGKTAAFALPILQALLEN--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 312 kKQYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGRENYKDQIhKLRLGCHILIATPGRLIDVMDQ--GLiGME 389
Cdd:cd17954 66 -PQRFFALVLAPTRELAQQISEQFEALGSSIGLKSAVLVGGMDMMAQAI-ALAKKPHVIVATPGRLVDHLENtkGF-SLK 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 226437753 390 GCRYLVLDEADRMLDMGFEPQIRQIVEcnRMPSkeERITAMFSATFPKEIQLL 442
Cdd:cd17954 143 SLKFLVMDEADRLLNMDFEPEIDKILK--VIPR--ERTTYLFSATMTTKVAKL 191
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
246-456 |
3.90e-46 |
|
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: 162.84 E-value: 3.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 246 IKTAGYDRPTPVQKYSIP-ALQGgRDLMSCAQTGSGKTAAFLVPLVnailqdgpDAVHRSVTSSG---GrkkqypsALVL 321
Cdd:cd17941 5 LKEAGFIKMTEIQRDSIPhALQG-RDILGAAKTGSGKTLAFLVPLL--------EKLYRERWTPEdglG-------ALII 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 322 SPTRELSLQIFNESRKFAYRTPITSALLYGGReNYKDQihKLRLG-CHILIATPGRLIDVMDQG-LIGMEGCRYLVLDEA 399
Cdd:cd17941 69 SPTRELAMQIFEVLRKVGKYHSFSAGLIIGGK-DVKEE--KERINrMNILVCTPGRLLQHMDETpGFDTSNLQMLVLDEA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 226437753 400 DRMLDMGFEPQIRQIVEcnRMPSKeeRITAMFSATFPKEIQLLAQDFLKeNYVFLAV 456
Cdd:cd17941 146 DRILDMGFKETLDAIVE--NLPKS--RQTLLFSATQTKSVKDLARLSLK-NPEYISV 197
|
|
| DEADc_DDX6 |
cd17940 |
DEAD-box helicase domain of DEAD box protein 6; DEAD box protein 6 (DDX6, also known as Rck or ... |
233-451 |
4.94e-46 |
|
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: 162.47 E-value: 4.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 233 FSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQdgpdavhrsvtssggrK 312
Cdd:cd17940 1 FEDYGLKRELLMGIFEKGFEKPSPIQEESIPIALSGRDILARAKNGTGKTGAYLIPILEKIDP----------------K 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 313 KQYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCR 392
Cdd:cd17940 65 KDVIQALILVPTRELALQTSQVCKELGKHMGVKVMVTTGG-TSLRDDIMRLYQTVHVLVGTPGRILDLAKKGVADLSHCK 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 226437753 393 YLVLDEADRMLDMGFEPQIRQIVecNRMPskEERITAMFSATFPKEIQLLAQDFLKENY 451
Cdd:cd17940 144 TLVLDEADKLLSQDFQPIIEKIL--NFLP--KERQILLFSATFPLTVKNFMDRHMHNPY 198
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
246-469 |
7.51e-46 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 161.89 E-value: 7.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 246 IKTAGYDRPTPVQKYSIP-ALQGGRDLMSCAQTGSGKTAAFLVPLVNAIlqdgpdavhrsvtssggRKKQYPSALVLSPT 324
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIEaLLSGLRDVILAAPTGSGKTLAALLPALEAL-----------------KRGKGGRVLVLVPT 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 325 RELSLQIFNESRKFAYRTPITSALLYGGrENYKDQIHKLRLGC-HILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRML 403
Cdd:smart00487 64 RELAEQWAEELKKLGPSLGLKVVGLYGG-DSKREQLRKLESGKtDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226437753 404 DMGFEPQIRQIveCNRMPSKeeRITAMFSATFPKEIQLLAQDFLKeNYVFLAVGRvgSTSENIMQK 469
Cdd:smart00487 143 DGGFGDQLEKL--LKLLPKN--VQLLLLSATPPEEIENLLELFLN-DPVFIDVGF--TPLEPIEQF 201
|
|
| DEADc_DDX59 |
cd17962 |
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ... |
245-449 |
1.37e-45 |
|
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: 161.18 E-value: 1.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 245 NIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQdgpdavhrsvtssggrKKQYPSALVLSPT 324
Cdd:cd17962 4 NLKKAGYEVPTPIQMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRCLT----------------EHRNPSALILTPT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 325 RELSLQIFNESRKFAYRTP-ITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRML 403
Cdd:cd17962 68 RELAVQIEDQAKELMKGLPpMKTALLVGG-LPLPPQLYRLQQGVKVIIATPGRLLDILKQSSVELDNIKIVVVDEADTML 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 226437753 404 DMGFEPQIRQIVEcnRMPSKEEriTAMFSATFPKEIQLLAQDFLKE 449
Cdd:cd17962 147 KMGFQQQVLDILE--NISHDHQ--TILVSATIPRGIEQLAGQLLQN 188
|
|
| DEADc_DDX41 |
cd17951 |
DEAD-box helicase domain of DEAD box protein 41; DDX41 (also called ABS and MPLPF) interacts ... |
246-447 |
3.55e-43 |
|
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: 154.80 E-value: 3.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 246 IKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQdgpdavhrSVTSSGGRKKQYPSALVLSPTR 325
Cdd:cd17951 5 LKKKGIKKPTPIQMQGLPTILSGRDMIGIAFTGSGKTLVFTLPLIMFALE--------QEKKLPFIKGEGPYGLIVCPSR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 326 ELSLQIFNESRKFAYR------TPITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEA 399
Cdd:cd17951 77 ELARQTHEVIEYYCKAlqeggyPQLRCLLCIGG-MSVKEQLEVIRKGVHIVVATPGRLMDMLNKKKINLDICRYLCLDEA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 226437753 400 DRMLDMGFEPQIRQIVECnrmpSKEERITAMFSATFPKEIQLLAQDFL 447
Cdd:cd17951 156 DRMIDMGFEEDIRTIFSY----FKGQRQTLLFSATMPKKIQNFAKSAL 199
|
|
| DEADc_DDX24 |
cd17946 |
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ... |
250-470 |
5.98e-41 |
|
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: 149.70 E-value: 5.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 250 GYDRPTPVQKYSIP-ALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQdgpdavHRSVTSSGGRKKqYPSALVLSPTRELS 328
Cdd:cd17946 9 GFSEPTPIQALALPaAIRDGKDVIGAAETGSGKTLAFGIPILERLLS------QKSSNGVGGKQK-PLRALILTPTRELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 329 LQIFNESRKFAYRTPITSALLYGGRENYKdQIHKLRLGCHILIATPGRLIDVMDQG---LIGMEGCRYLVLDEADRMLDM 405
Cdd:cd17946 82 VQVKDHLKAIAKYTNIKIASIVGGLAVQK-QERLLKKRPEIVVATPGRLWELIQEGnehLANLKSLRFLVLDEADRMLEK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226437753 406 G-FEpQIRQIVEC---NRMPSKEERITAMFSATFPKEIQLLAQDFLKENYVFLavgRVGSTSENIMQKI 470
Cdd:cd17946 161 GhFA-ELEKILELlnkDRAGKKRKRQTFVFSATLTLDHQLPLKLNSKKKKKKK---EKKQKLELLIEKV 225
|
|
| DEADc_DDX18 |
cd17942 |
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ... |
246-454 |
7.32e-41 |
|
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: 147.89 E-value: 7.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 246 IKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAIlqdgpdavhrsvTSSGGRKKQYPSALVLSPTR 325
Cdd:cd17942 5 IEEMGFTKMTEIQAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPAIELL------------YKLKFKPRNGTGVIIISPTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 326 ELSLQIFNESRKFAYRTPITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDVMD--QGLIgMEGCRYLVLDEADRML 403
Cdd:cd17942 73 ELALQIYGVAKELLKYHSQTFGIVIGG-ANRKAEAEKLGKGVNILVATPGRLLDHLQntKGFL-YKNLQCLIIDEADRIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 226437753 404 DMGFEPQIRQIVECnrMPSkeERITAMFSATFPKEIQLLAQDFLKENYVFL 454
Cdd:cd17942 151 EIGFEEEMRQIIKL--LPK--RRQTMLFSATQTRKVEDLARISLKKKPLYV 197
|
|
| DEADc_DDX1 |
cd17938 |
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ... |
233-434 |
8.40e-37 |
|
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: 137.07 E-value: 8.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 233 FSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVnailqdgpdavhrsvtssggrk 312
Cdd:cd17938 1 FEELGVMPELIKAVEELDWLLPTDIQAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 313 kQYPSALVLSPTRELSLQIFNESRKFAY--RTP-ITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGME 389
Cdd:cd17938 59 -QIVVALILEPSRELAEQTYNCIENFKKylDNPkLRVALLIGG-VKAREQLKRLESGVDIVVGTPGRLEDLIKTGKLDLS 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 226437753 390 GCRYLVLDEADRMLDMGFEPQIRQIVecNRMP---SKEERITAM-FSAT 434
Cdd:cd17938 137 SVRFFVLDEADRLLSQGNLETINRIY--NRIPkitSDGKRLQVIvCSAT 183
|
|
| DEADc_DDX56 |
cd17961 |
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ... |
246-448 |
1.29e-36 |
|
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: 136.56 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 246 IKTAGYDRPTPVQKYSIP-ALQGgRDLMSCAQTGSGKTAAFLVPLVNAILQDgpdavhrsvtSSGGRKKQYPSALVLSPT 324
Cdd:cd17961 9 IAKLGWEKPTLIQSKAIPlALEG-KDILARARTGSGKTAAYALPIIQKILKA----------KAESGEEQGTRALILVPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 325 RELSLQIFNESRKF-AYRTPITSALLYGGRENYKDQIHKLRLGCHILIATPGRLIDVMDQG-LIGMEGCRYLVLDEADRM 402
Cdd:cd17961 78 RELAQQVSKVLEQLtAYCRKDVRVVNLSASSSDSVQRALLAEKPDIVVSTPARLLSHLESGsLLLLSTLKYLVIDEADLV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 226437753 403 LDMGFEPQIRQIVEcnRMPskeeRITAMF--SATFPKEIQLLAQDFLK 448
Cdd:cd17961 158 LSYGYEEDLKSLLS--YLP----KNYQTFlmSATLSEDVEALKKLVLH 199
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
477-587 |
1.76e-36 |
|
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: 132.33 E-value: 1.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 477 EKRSYLMDLLDATGDSSlTLVFVETKRGAsDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAVAARGL 556
Cdd:pfam00271 1 EKLEALLELLKKERGGK-VLIFSQTKKTL-EAELLLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGL 78
|
90 100 110
....*....|....*....|....*....|.
gi 226437753 557 DIPNVKHVINYDLPSDVDEYVHRIGRTGRVG 587
Cdd:pfam00271 79 DLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| DEADc_EIF4A |
cd17939 |
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ... |
235-449 |
4.60e-36 |
|
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: 134.76 E-value: 4.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 235 DLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVplvnAILQDgPDAVHRSvtssggrkkq 314
Cdd:cd17939 1 DMGLSEDLLRGIYAYGFEKPSAIQQRAIVPIIKGRDVIAQAQSGTGKTATFSI----GALQR-IDTTVRE---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 315 yPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYL 394
Cdd:cd17939 66 -TQALVLAPTRELAQQIQKVVKALGDYMGVKVHACIGG-TSVREDRRKLQYGPHIVVGTPGRVFDMLQRRSLRTDKIKMF 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 226437753 395 VLDEADRMLDMGFEPQIRQIVecnRMPSKEERItAMFSATFPKEIQLLAQDFLKE 449
Cdd:cd17939 144 VLDEADEMLSRGFKDQIYDIF---QFLPPETQV-VLFSATMPHEVLEVTKKFMRD 194
|
|
| DEADc_EIF4AII_EIF4AI_DDX2 |
cd18046 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ... |
233-449 |
4.37e-32 |
|
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: 123.32 E-value: 4.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 233 FSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVplvnAILQDgpdaVHRSVTSsggrk 312
Cdd:cd18046 1 FDDMNLKESLLRGIYAYGFEKPSAIQQRAIMPCIKGYDVIAQAQSGTGKTATFSI----SILQQ----IDTSLKA----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 313 kqyPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCR 392
Cdd:cd18046 68 ---TQALVLAPTRELAQQIQKVVMALGDYMGIKCHACIGG-TSVRDDAQKLQAGPHIVVGTPGRVFDMINRRYLRTDYIK 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 226437753 393 YLVLDEADRMLDMGFEPQIRQIVEcnRMPSKEEriTAMFSATFPKEIQLLAQDFLKE 449
Cdd:cd18046 144 MFVLDEADEMLSRGFKDQIYDIFQ--KLPPDTQ--VVLLSATMPNDVLEVTTKFMRD 196
|
|
| DEADc_DDX21_DDX50 |
cd17944 |
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ... |
244-451 |
2.24e-31 |
|
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: 121.49 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 244 ENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDGPDAvhrsvtssggRKKQYPSALVLSP 323
Cdd:cd17944 3 KLLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPR----------KRGRAPKVLVLAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 324 TRELSLQIFNESRKFAYRtpITSALLYGGrENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRML 403
Cdd:cd17944 73 TRELANQVTKDFKDITRK--LSVACFYGG-TPYQQQIFAIRNGIDILVGTPGRIKDHLQNGRLDLTKLKHVVLDEVDQML 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 226437753 404 DMGFEPQIRQIV-ECNRMPSKEERITAMFSATFPKEIQLLAQDFLKENY 451
Cdd:cd17944 150 DMGFAEQVEEILsVSYKKDSEDNPQTLLFSATCPDWVYNVAKKYMKSQY 198
|
|
| DEADc_DDX19_DDX25 |
cd17963 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX19 and DDX25; DDX19 (also called ... |
246-448 |
5.58e-31 |
|
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: 119.99 E-value: 5.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 246 IKTAGYDRPTPVQKYSIPALQGG--RDLMSCAQTGSGKTAAFLVPLVNAIlqdgpDavhrsvtssggRKKQYPSALVLSP 323
Cdd:cd17963 9 LYAMGFNKPSKIQETALPLILSDppENLIAQSQSGTGKTAAFVLAMLSRV-----D-----------PTLKSPQALCLAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 324 TRELSLQIFNESRKFAYRTPITSALLYGGRENYKDQihklRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRML 403
Cdd:cd17963 73 TRELARQIGEVVEKMGKFTGVKVALAVPGNDVPRGK----KITAQIVIGTPGTVLDWLKKRQLDLKKIKILVLDEADVML 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 226437753 404 DM-GFEPQIRQIvecNRMPSKEERITaMFSATFPKEIQLLAQDFLK 448
Cdd:cd17963 149 DTqGHGDQSIRI---KRMLPRNCQIL-LFSATFPDSVRKFAEKIAP 190
|
|
| DEADc_DDX28 |
cd17948 |
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ... |
244-444 |
9.41e-31 |
|
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: 120.55 E-value: 9.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 244 ENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDgPDAVHRSVTSsggrkkqyPSALVLSP 323
Cdd:cd17948 3 EILQRQGITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLLRY-KLLAEGPFNA--------PRGLVITP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 324 TRELSLQIFNESRKFAYRTPITSALLYGGREnyKDQIHKLRLG-CHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRM 402
Cdd:cd17948 74 SRELAEQIGSVAQSLTEGLGLKVKVITGGRT--KRQIRNPHFEeVDILVATPGALSKLLTSRIYSLEQLRHLVLDEADTL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 226437753 403 LDMGFEPQIRQIVE-----CNRMPSKEERITA----MFSATFPKEI-QLLAQ 444
Cdd:cd17948 152 LDDSFNEKLSHFLRrfplaSRRSENTDGLDPGtqlvLVSATMPSGVgEVLSK 203
|
|
| DEADc_DDX39 |
cd17950 |
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ... |
231-448 |
2.44e-30 |
|
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: 118.60 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 231 SLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIP-ALQGGrDLMSCAQTGSGKTAAFLVPLVNAILQDGPDAvhrsvtssg 309
Cdd:cd17950 2 SGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPqAILGM-DVLCQAKSGMGKTAVFVLSTLQQLEPVDGQV--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 310 grkkqypSALVLSPTRELSLQIFNESRKFA-YRTPITSALLYGGRENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGM 388
Cdd:cd17950 72 -------SVLVICHTRELAFQISNEYERFSkYMPNVKTAVFFGGVPIKKDIEVLKNKCPHIVVGTPGRILALVREKKLKL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226437753 389 EGCRYLVLDEADRM---LDMGfepqiRQIVECNRMPSKEERITaMFSATFPKEIQLLAQDFLK 448
Cdd:cd17950 145 SHVKHFVLDECDKMleqLDMR-----RDVQEIFRATPHDKQVM-MFSATLSKEIRPVCKKFMQ 201
|
|
| DEADc_DDX20 |
cd17943 |
DEAD-box helicase domain of DEAD box protein 20; DDX20 (also called DEAD Box Protein DP 103, ... |
244-437 |
4.55e-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: 117.36 E-value: 4.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 244 ENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPlvnailqdgpdAVHRSVTSSGGrkkqyPSALVLSP 323
Cdd:cd17943 3 EGLKAAGFQRPSPIQLAAIPLGLAGHDLIVQAKSGTGKTLVFVVI-----------ALESLDLERRH-----PQVLILAP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 324 TRELSLQIFNESRKFA-YRTPITSALLYGGRENYKDQIhKLRlGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRM 402
Cdd:cd17943 67 TREIAVQIHDVFKKIGkKLEGLKCEVFIGGTPVKEDKK-KLK-GCHIAVGTPGRIKQLIELGALNVSHVRLFVLDEADKL 144
|
170 180 190
....*....|....*....|....*....|....*
gi 226437753 403 LDMGFEPQIRQIVecNRMPSKeeRITAMFSATFPK 437
Cdd:cd17943 145 MEGSFQKDVNWIF--SSLPKN--KQVIAFSATYPK 175
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
508-587 |
5.33e-29 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 110.38 E-value: 5.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 508 LAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVG 587
Cdd:smart00490 3 LAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
|
|
| DEADc_DDX51 |
cd17956 |
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ... |
244-408 |
6.26e-26 |
|
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: 106.56 E-value: 6.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 244 ENIKTAGYDRPTPVQKYSIPALQGG---------RDLMSCAQTGSGKTAAFLVPLVNAILQdgpdAVHRSVtssggrkkq 314
Cdd:cd17956 3 KNLQNNGITSAFPVQAAVIPWLLPSskstppyrpGDLCVSAPTGSGKTLAYVLPIVQALSK----RVVPRL--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 315 ypSALVLSPTRELSLQIFNESRKFAYRTPITSALLyGGRENYKDQIHKLRLGCH--------ILIATPGRLIDVMDQGL- 385
Cdd:cd17956 70 --RALIVVPTKELVQQVYKVFESLCKGTGLKVVSL-SGQKSFKKEQKLLLVDTSgrylsrvdILVATPGRLVDHLNSTPg 146
|
170 180
....*....|....*....|...
gi 226437753 386 IGMEGCRYLVLDEADRMLDMGFE 408
Cdd:cd17956 147 FTLKHLRFLVIDEADRLLNQSFQ 169
|
|
| DEADc_EIF4AIII_DDX48 |
cd18045 |
DEAD-box helicase domain of eukaryotic initiation factor 4A-III; Eukaryotic initiation factor ... |
233-454 |
1.06e-25 |
|
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: 105.24 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 233 FSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAIlqdgpDAVHRSvtssggrk 312
Cdd:cd18045 1 FETMGLREDLLRGIYAYGFEKPSAIQQRAIKPIIKGRDVIAQSQSGTGKTATFSISVLQCL-----DIQVRE-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 313 kqyPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGReNYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCR 392
Cdd:cd18045 68 ---TQALILSPTRELAVQIQKVLLALGDYMNVQCHACIGGT-SVGDDIRKLDYGQHIVSGTPGRVFDMIRRRSLRTRHIK 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226437753 393 YLVLDEADRMLDMGFEPQIRQIVEcnRMPSKEERItaMFSATFPKEIQLLAQDFLKENYVFL 454
Cdd:cd18045 144 MLVLDEADEMLNKGFKEQIYDVYR--YLPPATQVV--LVSATLPQDILEMTNKFMTDPIRIL 201
|
|
| DEADc_MRH4 |
cd17965 |
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 ... |
244-438 |
8.28e-20 |
|
DEAD-box helicase domain of ATP-dependent RNA helicase MRH4; Mitochondrial RNA helicase 4 (MRH4) plays an essential role during the late stages of mitochondrial ribosome or mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions. MRH4 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350723 [Multi-domain] Cd Length: 251 Bit Score: 89.36 E-value: 8.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 244 ENIKTAGYDRPTPVQKYSIPALQGGR----------------DLMSCAQTGSGKTAAFLVPLVNAILQDGPDAVHRSVTS 307
Cdd:cd17965 21 GSNKTDEEIKPSPIQTLAIKKLLKTLmrkvtkqtsneepkleVFLLAAETGSGKTLAYLAPLLDYLKRQEQEPFEEAEEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 308 SGGRKK-QYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGR-ENYKDQIHKLRLGCHILIATPGRLIDVMDQGL 385
Cdd:cd17965 101 YESAKDtGRPRSVILVPTHELVEQVYSVLKKLSHTVKLGIKTFSSGFgPSYQRLQLAFKGRIDILVTTPGKLASLAKSRP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 226437753 386 IGMEGCRYLVLDEADRMLDMGFEPQIRQIVEcnRMPSKEERItaMFSATFPKE 438
Cdd:cd17965 181 KILSRVTHLVVDEADTLFDRSFLQDTTSIIK--RAPKLKHLI--LCSATIPKE 229
|
|
| DEADc_DDX25 |
cd18048 |
DEAD-box helicase domain of DEAD box protein 25; DDX25 (also called gonadotropin-regulated ... |
219-444 |
3.56e-19 |
|
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: 87.00 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 219 VEATGDDVPQP---ISLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGG--RDLMSCAQTGSGKTAAFLVPLVNAI 293
Cdd:cd18048 3 VEVLQRDPTSPlfsVKSFEELHLKEELLRGIYAMGFNRPSKIQENALPMMLADppQNLIAQSQSGTGKTAAFVLAMLSRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 294 lqdgpDAvhrsvtssggrKKQYPSALVLSPTRELSLQ---IFNESRKFAYRTPITSAlLYGGRENYKDQIHKlrlgcHIL 370
Cdd:cd18048 83 -----DA-----------LKLYPQCLCLSPTFELALQtgkVVEEMGKFCVGIQVIYA-IRGNRPGKGTDIEA-----QIV 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226437753 371 IATPGRLID-VMDQGLIGMEGCRYLVLDEADRMLDM-GFEPQIRQIVECnrMPSKEERItaMFSATFPKEIQLLAQ 444
Cdd:cd18048 141 IGTPGTVLDwCFKLRLIDVTNISVFVLDEADVMINVqGHSDHSVRVKRS--MPKECQML--LFSATFEDSVWAFAE 212
|
|
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
247-609 |
5.56e-18 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 87.50 E-value: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 247 KTAGYDRPTPVQKYSIPALQGGRD---LMscaQTGSGKTAAFLVPlvnAILQDGPdavhrsvtssggrkkqypsALVLSP 323
Cdd:COG0514 11 RVFGYDSFRPGQEEIIEAVLAGRDalvVM---PTGGGKSLCYQLP---ALLLPGL-------------------TLVVSP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 324 TreLSL---QIfnES-RKF----AYrtpITSALLYGGRENYKDQIH--KLRLgchILIAtPGRL-----IDVMDQGLIGM 388
Cdd:COG0514 66 L--IALmkdQV--DAlRAAgiraAF---LNSSLSAEERREVLRALRagELKL---LYVA-PERLlnprfLELLRRLKISL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 389 egcryLVLDEA--------DrmldmgFEP---QIRQIVEcnRMPskeERITAMFSATFPKEIQ--LLAQDFLKENYVFLA 455
Cdd:COG0514 135 -----FAIDEAhcisqwghD------FRPdyrRLGELRE--RLP---NVPVLALTATATPRVRadIAEQLGLEDPRVFVG 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 456 -VGRvgstsENIMQKIVWVEEDEKRSYLMDLLDATGDSSlTLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKH 534
Cdd:COG0514 199 sFDR-----PNLRLEVVPKPPDDKLAQLLDFLKEHPGGS-GIVYCLSRKKVEELAEWLREAGIRAAAYHAGLDAEEREAN 272
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226437753 535 LDLFRTGTAPILVATaVA-ARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSFFNDKNRNIARELMD 609
Cdd:COG0514 273 QDRFLRDEVDVIVAT-IAfGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALLLYGPEDVAIQRFFIE 347
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
266-582 |
3.99e-17 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 85.08 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 266 QGGRDLMSCAQTGSGKT--AAFLVplvnAILQDGPdavhrsvtssggrkkqypSALVLSPTRELSLQIFNESRKFayrtp 343
Cdd:COG1061 98 RGGGRGLVVAPTGTGKTvlALALA----AELLRGK------------------RVLVLVPRRELLEQWAEELRRF----- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 344 ITSALLYGGRENykdqihklrLGCHILIATPGRLIDVMDQGLIGmEGCRYLVLDEADRmldmGFEPQIRQIVEcnRMPSK 423
Cdd:COG1061 151 LGDPLAGGGKKD---------SDAPITVATYQSLARRAHLDELG-DRFGLVIIDEAHH----AGAPSYRRILE--AFPAA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 424 eeRITAMfSAT------FPKEI-------------QLLAQDFLKEnYVFLAV--------GRVGSTSENIMQKIVwVEED 476
Cdd:COG1061 215 --YRLGL-TATpfrsdgREILLflfdgivyeyslkEAIEDGYLAP-PEYYGIrvdltderAEYDALSERLREALA-ADAE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 477 EKRSYLMDLLDATGDSSLTLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAVAARGL 556
Cdd:COG1061 290 RKDKILRELLREHPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGV 369
|
330 340
....*....|....*....|....*.
gi 226437753 557 DIPNVKHVINYDLPSDVDEYVHRIGR 582
Cdd:COG1061 370 DVPRLDVAILLRPTGSPREFIQRLGR 395
|
|
| MPH1 |
COG1111 |
ERCC4-related helicase [Replication, recombination and repair]; |
478-585 |
7.12e-15 |
|
ERCC4-related helicase [Replication, recombination and repair];
Pssm-ID: 440728 [Multi-domain] Cd Length: 718 Bit Score: 78.23 E-value: 7.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 478 KRSYLMDLLD---ATGDSSLTLVFVETKRGASDLAYYLNRQNYEVVTIHGD--------LKQFEREKHLDLFRTGTAPIL 546
Cdd:COG1111 336 KLSKLREILKeqlGTNPDSRIIVFTQYRDTAEMIVEFLSEPGIKAGRFVGQaskegdkgLTQKEQIEILERFRAGEFNVL 415
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 226437753 547 VATAVAARGLDIPNVKHVINYDL-PSDVdEYVHRIGRTGR 585
Cdd:COG1111 416 VATSVAEEGLDIPEVDLVIFYEPvPSEI-RSIQRKGRTGR 454
|
|
| DEADc_DDX19 |
cd18047 |
DEAD-box helicase domain of DEAD box protein 19; DDX19 is an RNA helicase involved in both ... |
233-444 |
6.96e-12 |
|
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: 65.13 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 233 FSDLSLHEWIEENIKTAGYDRPTPVQKYSIPAL--QGGRDLMSCAQTGSGKTAAFLVPLVNAIlqdGPDAvhrsvtssgg 310
Cdd:cd18047 3 FEELRLKPQLLQGVYAMGFNRPSKIQENALPLMlaEPPQNLIAQSQSGTGKTAAFVLAMLSQV---EPAN---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 311 rkkQYPSALVLSPTRELSLQIFNESRKFAYRTPITSaLLYGGRENYKDQihKLRLGCHILIATPGRLID-VMDQGLIGME 389
Cdd:cd18047 70 ---KYPQCLCLSPTYELALQTGKVIEQMGKFYPELK-LAYAVRGNKLER--GQKISEQIVIGTPGTVLDwCSKLKFIDPK 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 226437753 390 GCRYLVLDEADRMLdmGFEPQIRQIVECNRMPSKEERITaMFSATFPKEIQLLAQ 444
Cdd:cd18047 144 KIKVFVLDEADVMI--ATQGHQDQSIRIQRMLPRNCQML-LFSATFEDSVWKFAQ 195
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
274-434 |
4.82e-11 |
|
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: 61.27 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 274 CAQTGSGKTAAFLVPLVNAILQdgpdavhrsvtssgGRKKqypsALVLSPTRELSLQIFNESRKFaYRTPITSALLYGGR 353
Cdd:cd00046 7 TAPTGSGKTLAALLAALLLLLK--------------KGKK----VLVLVPTKALALQTAERLREL-FGPGIRVAVLVGGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 354 eNYKDQIHKLRLGCHILIATPGRLI-DVMDQGLIGMEGCRYLVLDEADRMLDMGFEPQIRQIVECNRMPSKEERITamFS 432
Cdd:cd00046 68 -SAEEREKNKLGDADIIIATPDMLLnLLLREDRLFLKDLKLIIVDEAHALLIDSRGALILDLAVRKAGLKNAQVIL--LS 144
|
..
gi 226437753 433 AT 434
Cdd:cd00046 145 AT 146
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
495-582 |
5.39e-11 |
|
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: 61.07 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 495 TLVFVETKRGASDLAYYL-------NRQNYEVVTIHGDLKQFEREKH--------LDLFRTGTAPILVATAVAARGLDIP 559
Cdd:cd18802 28 GIIFVERRATAVVLSRLLkehpstlAFIRCGFLIGRGNSSQRKRSLMtqrkqketLDKFRDGELNLLIATSVLEEGIDVP 107
|
90 100
....*....|....*....|...
gi 226437753 560 NVKHVINYDLPSDVDEYVHRIGR 582
Cdd:cd18802 108 ACNLVIRFDLPKTLRSYIQSRGR 130
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
234-617 |
1.02e-09 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 61.45 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 234 SDLSLhEWIEENIKTAGYDRPTPVQKYSIPA-LQGGRDLMSCAQTGSGKTA-AFLvPLVNAILQDGPdavhrsvtssggr 311
Cdd:COG1204 4 AELPL-EKVIEFLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLiAEL-AILKALLNGGK------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 312 kkqypsALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGREnykdqIHKLRLG-CHILIATPGRLIDVMDQGLIGMEG 390
Cdd:COG1204 69 ------ALYIVPLRALASEKYREFKRDFEELGIKVGVSTGDYD-----SDDEWLGrYDILVATPEKLDSLLRNGPSWLRD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 391 CRYLVLDEA------DRmldmGfePQIRQIVECNRMPSKEERITAMfSATF--PKEI-QLLAQDFLKENY--VFLAVGrV 459
Cdd:COG1204 138 VDLVVVDEAhliddeSR----G--PTLEVLLARLRRLNPEAQIVAL-SATIgnAEEIaEWLDAELVKSDWrpVPLNEG-V 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 460 GSTSENIMQKIVWVEEDEKRSYLMDLLDATGDsslTLVFVETKRGASDLAYYLNRQ------------------------ 515
Cdd:COG1204 210 LYDGVLRFDDGSRRSKDPTLALALDLLEEGGQ---VLVFVSSRRDAESLAKKLADElkrrltpeereeleelaeellevs 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 516 -----NYEVVTI--------HGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIPnVKHVI--------NYDLPsdVD 574
Cdd:COG1204 287 eethtNEKLADClekgvafhHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVNLP-ARRVIirdtkrggMVPIP--VL 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 226437753 575 EYVHRIGRTGR-----VGNVGLAtsffnDKNRNIARELMDLIVEANQE 617
Cdd:COG1204 364 EFKQMAGRAGRpgydpYGEAILV-----AKSSDEADELFERYILGEPE 406
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
237-592 |
3.46e-09 |
|
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: 60.23 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 237 SLHEWIEENIKTA----GYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDgPDAvhrsvtssggrk 312
Cdd:COG1205 36 PWPDWLPPELRAAlkkrGIERLYSHQAEAIEAARAGKNVVIATPTASGKSLAYLLPVLEALLED-PGA------------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 313 kqypSALVLSPTRELS------LQIFNEsrkfAYRTPITSALLYGGREnyKDQIHKLRLGCHILIATPgrliDVMDQGLI 386
Cdd:COG1205 103 ----TALYLYPTKALArdqlrrLRELAE----ALGLGVRVATYDGDTP--PEERRWIREHPDIVLTNP----DMLHYGLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 387 G--------MEGCRYLVLDEA---------------DRML----DMGFEPQIrqivecnrmpskeerITAmfSATF--PK 437
Cdd:COG1205 169 PhhtrwarfFRNLRYVVIDEAhtyrgvfgshvanvlRRLRricrHYGSDPQF---------------ILA--SATIgnPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 438 EiqlLAQDFLKENyvFLAVGRVGSTSeNIMQKIVW----VEEDEKRSYLMD----LLDATGDSSLTLVFVETKRGASDLA 509
Cdd:COG1205 232 E---HAERLTGRP--VTVVDEDGSPR-GERTFVLWnpplVDDGIRRSALAEaarlLADLVREGLRTLVFTRSRRGAELLA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 510 YYLNRQNYE---VVTI---HGDLKQFEREKHLDLFRTGTAPILVAT-AVAArGLDIPNVKHVINYDLPSDVDEYVHRIGR 582
Cdd:COG1205 306 RYARRALREpdlADRVaayRAGYLPEERREIERGLRSGELLGVVSTnALEL-GIDIGGLDAVVLAGYPGTRASFWQQAGR 384
|
410
....*....|
gi 226437753 583 TGRVGNVGLA 592
Cdd:COG1205 385 AGRRGQDSLV 394
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
545-590 |
5.98e-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: 53.09 E-value: 5.98e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 226437753 545 ILVATAVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVG 590
Cdd:cd18785 25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
474-586 |
7.66e-09 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 59.08 E-value: 7.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 474 EEDEKRSYLMDLLD---ATGDSslTLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAP--ILVA 548
Cdd:COG0553 530 GRSAKLEALLELLEellAEGEK--VLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEApvFLIS 607
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 226437753 549 TAVAARGLDIPNVKHVINYDLP--SDVDEY----VHRIGRTGRV 586
Cdd:COG0553 608 LKAGGEGLNLTAADHVIHYDLWwnPAVEEQaidrAHRIGQTRDV 651
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
482-581 |
1.58e-08 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 53.63 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 482 LMDLLDATGDSSL-TLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAP--ILVATAVAARGLDI 558
Cdd:cd18793 16 LLELLEELREPGEkVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIrvFLLSTKAGGVGLNL 95
|
90 100
....*....|....*....|....*....
gi 226437753 559 PNVKHVINYDLP--SDVDEY----VHRIG 581
Cdd:cd18793 96 TAANRVILYDPWwnPAVEEQaidrAHRIG 124
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
472-585 |
2.56e-08 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 53.42 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 472 WVEEDEKRSY--LMDLLDAtgdSSLTLVFVETKRGASDLAYYLNR---QNYEVVTI---HGDLKQFEREKHLDLFRTGTA 543
Cdd:cd18796 19 WAGESGADAYaeVIFLLER---HKSTLVFTNTRSQAERLAQRLRElcpDRVPPDFIalhHGSLSRELREEVEAALKRGDL 95
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 226437753 544 PILVATAVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGR 585
Cdd:cd18796 96 KVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGH 137
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
258-399 |
2.87e-08 |
|
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: 54.13 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 258 QKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDgpdavhrsvtsSGGRkkqypsALVLSPTRELSLQIFNESRK 337
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRD-----------PGSR------ALYLYPTKALAQDQLRSLRE 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226437753 338 FA-YRTPITSALLYGGRENYKDQIHKLRLGCHILIATPgrliDVMDQGLIG--------MEGCRYLVLDEA 399
Cdd:cd17923 68 LLeQLGLGIRVATYDGDTPREERRAIIRNPPRILLTNP----DMLHYALLPhhdrwarfLRNLRYVVLDEA 134
|
|
| PRK13766 |
PRK13766 |
Hef nuclease; Provisional |
467-589 |
7.70e-08 |
|
Hef nuclease; Provisional
Pssm-ID: 237496 [Multi-domain] Cd Length: 773 Bit Score: 55.65 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 467 MQKIV--WVEEDE---KRSYLMDLLDAT---GDSSLTLVFVETKRGASDLAYYLNRQNYEVVTIHGD--------LKQFE 530
Cdd:PRK13766 332 FRKAVrkAKELDIehpKLEKLREIVKEQlgkNPDSRIIVFTQYRDTAEKIVDLLEKEGIKAVRFVGQaskdgdkgMSQKE 411
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226437753 531 REKHLDLFRTGTAPILVATAVAARGLDIPNVKHVINYD-LPSDVdEYVHRIGRTGR--VGNV 589
Cdd:PRK13766 412 QIEILDKFRAGEFNVLVSTSVAEEGLDIPSVDLVIFYEpVPSEI-RSIQRKGRTGRqeEGRV 472
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
526-585 |
2.03e-07 |
|
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: 50.82 E-value: 2.03e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 526 LKQFEREKHLDLFRTGTAPILVATAVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGR 585
Cdd:cd18801 74 MSQKEQKEVIEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR 133
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
495-587 |
4.60e-07 |
|
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: 49.51 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 495 TLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIPNVKHVINYDLPSDVD 574
Cdd:cd18794 33 GIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFVIHYSLPKSME 112
|
90
....*....|...
gi 226437753 575 EYVHRIGRTGRVG 587
Cdd:cd18794 113 SYYQESGRAGRDG 125
|
|
| SF2_C_XPB |
cd18789 |
C-terminal helicase domain of XPB-like helicases; TFIIH basal transcription factor complex ... |
484-596 |
8.30e-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: 49.17 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 484 DLLDATGDSSLTLVFVETKrgaSDLAYYLNRQNYEVVTihGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIP--NV 561
Cdd:cd18789 41 ELLKRHEQGDKIIVFTDNV---EALYRYAKRLLKPFIT--GETPQSEREEILQNFREGEYNTLVVSKVGDEGIDLPeaNV 115
|
90 100 110
....*....|....*....|....*....|....*
gi 226437753 562 KHVINYDLPSDvDEYVHRIGRTGRVGNVGLATSFF 596
Cdd:cd18789 116 AIQISGHGGSR-RQEAQRLGRILRPKKGGGKNAFF 149
|
|
| SF2_C_reverse_gyrase |
cd18798 |
C-terminal helicase domain of the reverse gyrase; Reverse gyrase modifies the topological ... |
471-591 |
1.02e-06 |
|
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: 49.23 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 471 VWVEEDEKRSYLMDLLDATGDSslTLVFVETKRG---ASDLAYYLNRQNYEVVTIHGDlkqfeREKHLDLFRTGTAPILV 547
Cdd:cd18798 5 VYIEDSDSLEKLLELVKKLGDG--GLIFVSIDYGkeyAEELKEFLERHGIKAELALSS-----TEKNLEKFEEGEIDVLI 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 226437753 548 ATA----VAARGLDIPN-VKHVINYDLPsdVDEYVHRIGRTGRVGNVGL 591
Cdd:cd18798 78 GVAsyygVLVRGIDLPErIKYAIFYGVP--VTTYIQASGRTSRLYAGGL 124
|
|
| Lhr |
COG1201 |
Lhr-like helicase [Replication, recombination and repair]; |
227-587 |
2.39e-06 |
|
Lhr-like helicase [Replication, recombination and repair];
Pssm-ID: 440814 [Multi-domain] Cd Length: 850 Bit Score: 50.87 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 227 PQPISLFSDLsLHEWIEENiktagYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKT-AAFLVPLVNAILQDGPDAVHRSV 305
Cdd:COG1201 4 EDVLSLLHPA-VRAWFAAR-----FGAPTPPQREAWPAIAAGESTLLIAPTGSGKTlAAFLPALDELARRPRPGELPDGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 306 TssggrkkqypsALVLSPTRELSlqifNESRKfAYRTPITsallyGGRENYKDQIHKLRLG------------------C 367
Cdd:COG1201 78 R-----------VLYISPLKALA----NDIER-NLRAPLE-----EIGEAAGLPLPEIRVGvrtgdtpaserqrqrrrpP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 368 HILIATP-----------GRLIdvmdqgligMEGCRYLVLDEadrmldmgfepqIRQIVEcnrmpSKE--------ERIT 428
Cdd:COG1201 137 HILITTPeslallltspdAREL---------LRGVRTVIVDE------------IHALAG-----SKRgvhlalslERLR 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 429 AM---------FSATFpKEIQLLAqDFL-----KENYVFLAVG-------RVGSTSENIMQKIVWVEEDEKRSY--LMDL 485
Cdd:COG1201 191 ALaprplqrigLSATV-GPLEEVA-RFLvgyedPRPVTIVDAGagkkpdlEVLVPVEDLIERFPWAGHLWPHLYprVLDL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 486 LDAtgdSSLTLVFVETKRGASDLAYYLNRQNYEVVTI----HGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIPNV 561
Cdd:COG1201 269 IEA---HRTTLVFTNTRSQAERLFQRLNELNPEDALPiaahHGSLSREQRLEVEEALKAGELRAVVATSSLELGIDIGDV 345
|
410 420
....*....|....*....|....*..
gi 226437753 562 KHVINYDLPSDVDEYVHRIGRTG-RVG 587
Cdd:COG1201 346 DLVIQVGSPKSVARLLQRIGRAGhRVG 372
|
|
| SF2_C_UvrB |
cd18790 |
C-terminal helicase domain of the UvrB family helicases; Excinuclease ABC subunit B (or UvrB) ... |
495-585 |
3.63e-06 |
|
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: 47.63 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 495 TLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIPNVKHVINYD-----L 569
Cdd:cd18790 30 VLVTTLTKRMAEDLTEYLQELGVKVRYLHSEIDTLERVEIIRDLRLGEFDVLVGINLLREGLDLPEVSLVAILDadkegF 109
|
90
....*....|....*.
gi 226437753 570 PSDVDEYVHRIGRTGR 585
Cdd:cd18790 110 LRSETSLIQTIGRAAR 125
|
|
| SF2_C_EcoAI-like |
cd18799 |
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family ... |
495-565 |
3.65e-06 |
|
C-terminal helicase domain of EcoAI HsdR-like restriction enzyme family helicases; This family is composed of helicase restriction enzymes, including the HsdR subunit of restriction-modification enzymes such as Escherichia coli type I restriction enzyme EcoAI R protein (R.EcoAI). The EcoAI enzyme recognizes 5'-GAGN(7)GTCA-3'. The HsdR or R subunit is required for both nuclease and ATPase activities, but not for modification. These proteins are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350186 [Multi-domain] Cd Length: 116 Bit Score: 46.40 E-value: 3.65e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226437753 495 TLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFERE---KHLDLFRTGTAPILVATAVAARGLDIPNVKHVI 565
Cdd:cd18799 9 TLIFCVSIEHAEFMAEAFNEAGIDAVALNSDYSDRERGdeaLILLFFGELKPPILVTVDLLTTGVDIPEVDNVV 82
|
|
| SF2_C_RecG |
cd18811 |
C-terminal helicase domain of DNA helicase RecG; ATP-dependent DNA helicase RecG plays a ... |
505-613 |
4.51e-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: 47.34 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 505 ASDLAYYLN---RQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIPNVKHVINYDlpsdvdeyVHRIG 581
Cdd:cd18811 47 AVAMYEYLKerfRPELNVGLLHGRLKSDEKDAVMAEFREGEVDILVSTTVIEVGVDVPNATVMVIED--------AERFG 118
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 226437753 582 RT------GRVGNVGLATSFF---NDKNRNIARELMDLIVE 613
Cdd:cd18811 119 LSqlhqlrGRVGRGDHQSYCLlvyKDPLTETAKQRLRVMTE 159
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
264-399 |
5.87e-06 |
|
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: 47.26 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 264 ALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQdgpdavhrsvtsSGGRkkqypsALVLSPTRELSLQIFNESRKFAYRTP 343
Cdd:cd17921 13 LYLSGDSVLVSAPTSSGKTLIAELAILRALAT------------SGGK------AVYIAPTRALVNQKEADLRERFGPLG 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 226437753 344 ITSALLYGgreNYKDQIHKLRlGCHILIATPGRLiDVM--DQGLIGMEGCRYLVLDEA 399
Cdd:cd17921 75 KNVGLLTG---DPSVNKLLLA-EADILVATPEKL-DLLlrNGGERLIQDVRLVVVDEA 127
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
498-587 |
1.57e-05 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 48.17 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 498 FVETKRGASDLAYYLNRQNYEVVT------------IHGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIPNVKHVI 565
Cdd:PRK11057 230 YVQEQRGKSGIIYCNSRAKVEDTAarlqsrgisaaaYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVV 309
|
90 100
....*....|....*....|..
gi 226437753 566 NYDLPSDVDEYVHRIGRTGRVG 587
Cdd:PRK11057 310 HFDIPRNIESYYQETGRAGRDG 331
|
|
| PRK13767 |
PRK13767 |
ATP-dependent helicase; Provisional |
240-286 |
7.70e-05 |
|
ATP-dependent helicase; Provisional
Pssm-ID: 237497 [Multi-domain] Cd Length: 876 Bit Score: 46.03 E-value: 7.70e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 226437753 240 EWIEENiktagYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKT-AAFL 286
Cdd:PRK13767 24 EWFKEK-----FGTFTPPQRYAIPLIHEGKNVLISSPTGSGKTlAAFL 66
|
|
| COG1202 |
COG1202 |
Superfamily II helicase, archaea-specific [Replication, recombination and repair]; |
200-290 |
1.50e-04 |
|
Superfamily II helicase, archaea-specific [Replication, recombination and repair];
Pssm-ID: 440815 [Multi-domain] Cd Length: 790 Bit Score: 45.27 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 200 ELFSGQLSgINFDKYEEIpvEATGDDVPqPISLfSDLSLHEWIEENIKTAGyDRPTPVQKYSIPA-LQGGRDLMSCAQTG 278
Cdd:COG1202 162 NLLSGRLD-PDLTKFDEI--SATTDEVD-TVPV-DDLDLPPELKDLLEGRG-EELLPVQSLAVENgLLEGKDQLVVSATA 235
|
90 100
....*....|....*....|....*....
gi 226437753 279 SGKT-----AA------------FLVPLV 290
Cdd:COG1202 236 TGKTligelAGiknalegkgkmlFLVPLV 264
|
|
| cas3_core |
TIGR01587 |
CRISPR-associated helicase Cas3; This model represents the highly conserved core region of an ... |
270-618 |
4.14e-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: 43.21 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 270 DLMSCAQTGSGKTAAFLVPLVNAILQDGPD-------------AVHRSV-------------TSSGGRKKQYPSALVLSp 323
Cdd:TIGR01587 1 LLVIEAPTGYGKTEAALLWALHSIKSQKADrviialptratinAMYRRAkelfgselvglhhSSSFSRIKEMGDSEEFE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 324 tRELSLQIFNESRKFAYRTPITSallyggrenyKDQIHKLRLGC--HILIATPGRLIDVmdqgligmegcryLVLDEADr 401
Cdd:TIGR01587 80 -HLFPLYIHSNDKLFLDPITVCT----------IDQVLKSVFGEfgHYEFTLASIANSL-------------LIFDEVH- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 402 mldmGFEPQIRQIVECNRMPSKEERITAM-FSATFPKeiqLLAQDFLKENYVFLAVGRVGSTSENIMQKIVWVEEDEKR- 479
Cdd:TIGR01587 135 ----FYDEYTLALILAVLEVLKDNDVPILlMSATLPK---FLKEYAEKIGYVEFNEPLDLKEERRFENHRFILIESDKVg 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 480 --SYLMDLLDATGDSSLTLVFVETKRGAsdLAYYLNRQ----NYEVVTIHGDLKQFEREKH-----LDLFRTGTAPILVA 548
Cdd:TIGR01587 208 eiSSLERLLEFIKKGGSIAIIVNTVDRA--QEFYQQLKekapEEEIILYHSRFTEKDRAKKeaellREMKKSNEKFVIVA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 549 TAVAARGLDipnvkhvINYDL----PSDVDEYVHRIGRTGRVG-------NVGLATSFFNDKNRNIARELMDLIVEANQE 617
Cdd:TIGR01587 286 TQVIEASLD-------ISADVmiteLAPIDSLIQRLGRLHRYGrkigenfEVYIITIAPEGKLFPYPYELVERTIQKLEE 358
|
.
gi 226437753 618 L 618
Cdd:TIGR01587 359 S 359
|
|
| DEXHc_RecG |
cd17918 |
DEXH/Q-box helicase domain of DEAD-like helicase RecG family proteins; The DEAD-like helicase ... |
253-372 |
1.03e-03 |
|
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: 40.48 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 253 RPTPVQKYSIPALQGG------RDLMSCAQTGSGKTAAFLVPLVNAIlqdgpdavhrsvtsSGGRkkqypSALVLSPTRE 326
Cdd:cd17918 15 SLTKDQAQAIKDIEKDlhspepMDRLLSGDVGSGKTLVALGAALLAY--------------KNGK-----QVAILVPTEI 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 226437753 327 LSLQIFNESRKFAyrTPITSALLYGGRENYKDQIHKLRLGCHILIA 372
Cdd:cd17918 76 LAHQHYEEARKFL--PFINVELVTGGTKAQILSGISLLVGTHALLH 119
|
|
| Cas3_I |
cd09639 |
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ... |
270-587 |
1.54e-03 |
|
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I
Pssm-ID: 187770 [Multi-domain] Cd Length: 353 Bit Score: 41.26 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 270 DLMSCAQTGSGKTAAFLVPLVNAILQDGPD-------------AVHRSVTSSGGRKKQYPSALVLSPT----------RE 326
Cdd:cd09639 1 LLVIEAPTGYGKTEAALLWALHSLKSQKADrviialptratinAMYRRAKEAFGETGLYHSSILSSRIkemgdseefeHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 327 LSLQIFNESRKFAYRTPITSallyggrenyKDQIHKLRLGC--HILIATPGRLIDVmdqgligmegcryLVLDEADrmld 404
Cdd:cd09639 81 FPLYIHSNDTLFLDPITVCT----------IDQVLKSVFGEfgHYEFTLASIANSL-------------LIFDEVH---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 405 mGFEPQIRQIVECNRMPSKEERITAM-FSATFPKeiqLLAQDFLKENYVFLAVGRVgsTSENIMQKIVWVEED--EKRSY 481
Cdd:cd09639 134 -FYDEYTLALILAVLEVLKDNDVPILlMSATLPK---FLKEYAEKIGYVEENEPLD--LKPNERAPFIKIESDkvGEISS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 482 LMDLLDATGDSSLTLVFVETKRGASDLAYYLNRQNYE--VVTIHGDLKQFEREKH----LDLFRTGTAPILVATAVAARG 555
Cdd:cd09639 208 LERLLEFIKKGGSVAIIVNTVDRAQEFYQQLKEKGPEeeIMLIHSRFTEKDRAKKeaelLLEFKKSEKFVIVATQVIEAS 287
|
330 340 350
....*....|....*....|....*....|....*.
gi 226437753 556 LDipnvkhvINYDL----PSDVDEYVHRIGRTGRVG 587
Cdd:cd09639 288 LD-------ISVDVmiteLAPIDSLIQRLGRLHRYG 316
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
243-399 |
2.19e-03 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 39.83 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 243 EENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPlvnAILQDGPdavhrsvtssggrkkqypsALVLS 322
Cdd:cd17920 2 QILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLP---ALLLDGV-------------------TLVVS 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 323 PTreLSL---QIFNESRKFAYRTPITSALLYGGRENYKDQIHKLRLgcHILIATPGRLIDVMDQGLIG----MEGCRYLV 395
Cdd:cd17920 60 PL--ISLmqdQVDRLQQLGIRAAALNSTLSPEEKREVLLRIKNGQY--KLLYVTPERLLSPDFLELLQrlpeRKRLALIV 135
|
....
gi 226437753 396 LDEA 399
Cdd:cd17920 136 VDEA 139
|
|
| SF2_C_RecG_TRCF |
cd18792 |
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family ... |
516-561 |
2.33e-03 |
|
C-terminal helicase domain of the RecG family helicases; The DEAD-like helicase RecG family contains recombination factor RecG and transcription-repair coupling factor TrcF. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350179 [Multi-domain] Cd Length: 160 Bit Score: 39.17 E-value: 2.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 226437753 516 NYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIPNV 561
Cdd:cd18792 60 EARVALLHGKMTEDEKEAVMLEFREGEYDILVSTTVIEVGIDVPNA 105
|
|
| SF2_C_priA |
cd18804 |
C-terminal helicase domain of ATP-dependent helicase PriA; PriA, also known as replication ... |
527-565 |
6.67e-03 |
|
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: 38.77 E-value: 6.67e-03
10 20 30
....*....|....*....|....*....|....*....
gi 226437753 527 KQFEREKHLDLFRTGTAPILVATAVAARGLDIPNVKHVI 565
Cdd:cd18804 129 KKGALEKLLDQFERGEIDILIGTQMIAKGLDFPNVTLVG 167
|
|
| DEXHc_archSki2 |
cd18028 |
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ... |
256-439 |
6.98e-03 |
|
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350786 [Multi-domain] Cd Length: 177 Bit Score: 38.08 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 256 PVQKYSIPA-LQGGRDLMSCAQTGSGKTAAFLVPLVNAILQdgpdavhrsvtssGGRkkqypsALVLSPTRELSLQIFNE 334
Cdd:cd18028 4 PPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLLE-------------GGK------ALYLVPLRALASEKYEE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226437753 335 SRKFaYRTPITSALLYGGRENYKDQIHKlrlgCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRMLDMGFEPQIRQI 414
Cdd:cd18028 65 FKKL-EEIGLKVGISTGDYDEDDEWLGD----YDIIVATYEKFDSLLRHSPSWLRDVGVVVVDEIHLISDEERGPTLESI 139
|
170 180
....*....|....*....|....*..
gi 226437753 415 VECNRMPSKEERITAMfSATF--PKEI 439
Cdd:cd18028 140 VARLRRLNPNTQIIGL-SATIgnPDEL 165
|
|
| |
