|
Name |
Accession |
Description |
Interval |
E-value |
| HrpA |
COG1643 |
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis]; |
497-1111 |
1.55e-180 |
|
HrpA-like RNA helicase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441249 [Multi-domain] Cd Length: 836 Bit Score: 551.61 E-value: 1.55e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGGNLGEEVGY 576
Cdd:COG1643 10 LPVSAVLPELLAALRAHQVVVLAAPPGAGKTTQLPLALLELGWGAGGRIGMLEPRRLAARAAAERMAEELGEPVGETVGY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 577 AIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVAR-RSDLKLIVTSATMDAE 655
Cdd:COG1643 90 RVRFEDKVSAATRIEVVTEGILLRELQRDPELEGVDTVIFDEFHERSLNADLLLALLLDLQPAlRPDLKLLVMSATLDAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 656 KFAAFFGNVPIFHIPGRTFPVDILF-----SKTPQEDYVEAAVKQSLQVHlsgaPGDILIFMPGQEDIEVTSDQIVEHLe 730
Cdd:COG1643 170 RFARLLGDAPVIESSGRTYPVEVRYrplpaDERDLEDAVADAVREALAEE----PGDILVFLPGEREIRRTAEALRGRL- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 731 elenAPALAVLPIYSQLPSDLQAKIFQKAPDGVRKCIVATNIAETSLTVDGIMFVIDSGYCKLKVFNPRIGMDALQIYPI 810
Cdd:COG1643 245 ----PPDTEILPLYGRLSAAEQDRAFAPAPHGRRRIVLATNIAETSLTVPGIRYVIDSGLARIPRYDPRSGVTRLPTERI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 811 SQANANQRSGRAGRTGPGQCFRLYTQSAYKNeLLTTTVPEIQRTNLANVVLLLKSLGVQDLLQFHFMDPPPEDNmLNSMY 890
Cdd:COG1643 321 SQASANQRAGRAGRLAPGICYRLWSEEDFAR-RPAFTDPEILRADLASLILELAAWGLGDPEDLPFLDPPPARA-IADAR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 891 QLWI-LGALDNTGGLTSTGRLMVEFPLDPALSKMLIVSCDMGCSSEILLIVSMLSVPaifyrpkgreeesDQIRekfAVP 969
Cdd:COG1643 399 ALLQeLGALDADGRLTPLGRALARLPLDPRLARMLLAAAELGCLREAAILAALLSER-------------DPRR---GAA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 970 ESDHLTYLNVYLQWKNNnystiwcNDHFIHAKAMRKVREVRAQLKDiMVQQRMSLASCGTDWdiVRKCICAAYFHQ-AAK 1048
Cdd:COG1643 463 GSDLLARLNLWRRLREQ-------QREFLSYLRLREWRDLARQLRR-LLGEGANEEPADYEA--IGLLLALAYPDRiARR 532
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034596784 1049 LKGIGEYVNIRtGMPCHLHPTSSLFGmgytPDYIVYHELVMTTKEY-MQCVTAVDGEWLAELGP 1111
Cdd:COG1643 533 RGEGGRYLLAR-GRGAALFPGSPLAK----KEWLVAAELVGGAAEArIRLAAPIDPEWLEELAA 591
|
|
| DEAH_box_HrpA |
TIGR01967 |
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ... |
445-1111 |
1.47e-152 |
|
RNA helicase HrpA; This model represents HrpA, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria and a few high-GC Gram-positive bacteria. HrpA is about 1300 amino acids long, while its paralog HrpB, also uncharacterized, is about 800 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. The HrpA/B homolog from Borrelia is 500 amino acids shorter but appears to be derived from HrpA rather than HrpB. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273900 [Multi-domain] Cd Length: 1283 Bit Score: 490.82 E-value: 1.47e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 445 GVKKEEEPDKAVTEDGKVDYRTEQKFADHMKRkseassefAKKKSILEQRQYLPIFAVQQELLTIIRDNSIVIVVGETGS 524
Cdd:TIGR01967 22 KLRKDHDQDRAIAALAKFRERIDAACDKVEAR--------RQAVPEIRYPDNLPVSAKREDIAEAIAENQVVIIAGETGS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 525 GKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGGNLGEEVGYAIRFEDCTSENTLIKYMTDGILLRESLR 604
Cdd:TIGR01967 94 GKTTQLPKICLELGRGSHGLIGHTQPRRLAARTVAQRIAEELGTPLGEKVGYKVRFHDQVSSNTLVKLMTDGILLAETQQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 605 EADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLIVTSATMDAEKFAAFFGNVPIFHIPGRTFPVDI----LF 680
Cdd:TIGR01967 174 DRFLSRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKIIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVryrpLV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 681 SKT-PQEDYVEAAVKQSLQVHLSGAPGDILIFMPGQEDIEVTSDQIVEHleeleNAPALAVLPIYSQLPSDLQAKIFQka 759
Cdd:TIGR01967 254 EEQeDDDLDQLEAILDAVDELFAEGPGDILIFLPGEREIRDAAEILRKR-----NLRHTEILPLYARLSNKEQQRVFQ-- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 760 PDGVRKCIVATNIAETSLTVDGIMFVIDSGYCKLKVFNPRIGMDALQIYPISQANANQRSGRAGRTGPGQCFRLYTQSAY 839
Cdd:TIGR01967 327 PHSGRRIVLATNVAETSLTVPGIHYVIDTGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVAPGICIRLYSEEDF 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 840 KNELLTTTvPEIQRTNLANVVLLLKSLGVQDLLQFHFMDPPPEDNMLNSMYQLWILGALDNTGG---LTSTGRLMVEFPL 916
Cdd:TIGR01967 407 NSRPEFTD-PEILRTNLASVILQMLALRLGDIAAFPFIEAPDPRAIRDGFRLLEELGALDDDEAepqLTPIGRQLAQLPV 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 917 DPALSKMLIVSCDMGCSSEILLIVSMLSVPAIFYRPKGREEESDQIREKFAVPESDHLTYLNV--YLQWKNNNYSTI--- 991
Cdd:TIGR01967 486 DPRLARMLLEAHRLGCLQEVLIIASALSIQDPRERPMEKQQAADQAHARFKDPRSDFLSRVNLwrHIEEQRQALSANqfr 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 992 -WCNDHFIHAKAMRKVREVRAQLKDIMVQQRMSLASCGTDWDIVRKCICAAYFHQAAKLKGIGEYVNIRtGMPCHLHPTS 1070
Cdd:TIGR01967 566 nACRKQYLNYLRVREWQDIYRQLTQVVKELGLKLNEEPADYDAIHKALLSGLLSQIGMKDEKHEYDGAR-GRKFHIFPGS 644
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1034596784 1071 SLFGMGytPDYIVYHELVMTTKEYMQCVTAVDGEWLAELGP 1111
Cdd:TIGR01967 645 PLFKKP--PKWVMAAELVETSKLYARLVAKIEPEWVEPVAG 683
|
|
| PRK11131 |
PRK11131 |
ATP-dependent RNA helicase HrpA; Provisional |
479-1109 |
1.05e-137 |
|
ATP-dependent RNA helicase HrpA; Provisional
Pssm-ID: 182986 [Multi-domain] Cd Length: 1294 Bit Score: 451.05 E-value: 1.05e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 479 EASSEFAKKKSILEQRQY----------LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCT 548
Cdd:PRK11131 45 EIAKEIAQAAQRVLLREAarpeitypenLPVSQKKQDILEAIRDHQVVIVAGETGSGKTTQLPKICLELGRGVKGLIGHT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 549 QPRRVAAMSVAKRVSEEMGGNLGEEVGYAIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDV 628
Cdd:PRK11131 125 QPRRLAARTVANRIAEELETELGGCVGYKVRFNDQVSDNTMVKLMTDGILLAEIQQDRLLMQYDTIIIDEAHERSLNIDF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 629 LFGLLREVVARRSDLKLIVTSATMDAEKFAAFFGNVPIFHIPGRTFPVDILFSKTPQEDyvEAAVKQSLQ-----VHLSG 703
Cdd:PRK11131 205 ILGYLKELLPRRPDLKVIITSATIDPERFSRHFNNAPIIEVSGRTYPVEVRYRPIVEEA--DDTERDQLQaifdaVDELG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 704 A--PGDILIFMPGQEDIEVTSDQivehLEELeNAPALAVLPIYSQLPSDLQAKIFQkaPDGVRKCIVATNIAETSLTVDG 781
Cdd:PRK11131 283 RegPGDILIFMSGEREIRDTADA----LNKL-NLRHTEILPLYARLSNSEQNRVFQ--SHSGRRIVLATNVAETSLTVPG 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 782 IMFVIDSGYCKLKVFNPRIGMDALQIYPISQANANQRSGRAGRTGPGQCFRLYTQSAYKN--ELlttTVPEIQRTNLANV 859
Cdd:PRK11131 356 IKYVIDPGTARISRYSYRTKVQRLPIEPISQASANQRKGRCGRVSEGICIRLYSEDDFLSrpEF---TDPEILRTNLASV 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 860 VLLLKSLGVQDLLQFHFMDPPPEDNMLNSMYQLWILGALDNTGG-----LTSTGRLMVEFPLDPALSKMLIVSCDMGCSS 934
Cdd:PRK11131 433 ILQMTALGLGDIAAFPFVEAPDKRNIQDGVRLLEELGAITTDEQasaykLTPLGRQLAQLPVDPRLARMVLEAQKHGCVR 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 935 EILLIVSMLSVPAIFYRPKGREEESDQIREKFAVPESDHLTYLNV--YLQWKNNNYSTI----WCNDHFIHAKAMRKVRE 1008
Cdd:PRK11131 513 EVMIITSALSIQDPRERPMDKQQASDEKHRRFADKESDFLAFVNLwnYLQEQQKALSSNqfrrLCRTDYLNYLRVREWQD 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 1009 VRAQLKDIMVQQRMSLASCGTDWDIVRKCICAAYF-HQAAKLKGIGEYVNIRTGMpCHLHPTSSLFGMgyTPDYIVYHEL 1087
Cdd:PRK11131 593 IYTQLRQVVKELGIPVNSEPAEYREIHTALLTGLLsHIGMKDAEKQEYTGARNAR-FSIFPGSGLFKK--PPKWVMVAEL 669
|
650 660
....*....|....*....|..
gi 1034596784 1088 VMTTKEYMQCVTAVDGEWLAEL 1109
Cdd:PRK11131 670 VETSRLWGRIAARIEPEWIEPL 691
|
|
| DEXHc_DHX38 |
cd17983 |
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as ... |
497-669 |
1.29e-120 |
|
DEXH-box helicase domain of DEAH-box helicase 38; DEAH-box helicase 38 (DHX38, also known as PRP16) is involved in pre-mRNA splicing. DHX38 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350741 [Multi-domain] Cd Length: 173 Bit Score: 369.48 E-value: 1.29e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGGNLGEEVGY 576
Cdd:cd17983 1 LPIFAVRQELLNVIRDNNVVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGVELGEEVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 577 AIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLIVTSATMDAEK 656
Cdd:cd17983 81 AIRFEDCTSENTVIKYMTDGILLRESLRDPDLDKYSAIIMDEAHERSLNTDVLFGLLREVVARRRDLKLIVTSATMDADK 160
|
170
....*....|...
gi 1034596784 657 FAAFFGNVPIFHI 669
Cdd:cd17983 161 FADFFGNVPIFTI 173
|
|
| DEAH_box_HrpB |
TIGR01970 |
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but ... |
497-948 |
1.30e-97 |
|
ATP-dependent helicase HrpB; This model represents HrpB, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria, but also in a few species of other lineages. The member from Rhizobium meliloti has been designated HelO. HrpB is typically about 800 residues in length, while its paralog HrpA (TIGR01967), also uncharacterized, is about 1300 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273901 [Multi-domain] Cd Length: 819 Bit Score: 330.19 E-value: 1.30e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLT-QYLHEDGYTdyGMIGCTQPRRVAAMSVAKRVSEEMGGNLGEEVG 575
Cdd:TIGR01970 1 LPIHAVLPALRDALAAHPQVVLEAPPGAGKSTAVPlALLDAPGIG--GKIIMLEPRRLAARSAAQRLASQLGEAVGQTVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 576 YAIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREV-VARRSDLKLIVTSATMDA 654
Cdd:TIGR01970 79 YRVRGENKVSRRTRLEVVTEGILTRMIQDDPELDGVGALIFDEFHERSLDADLGLALALDVqSSLREDLKILAMSATLDG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 655 EKFAAFFGNVPIFHIPGRTFPVDILFSKTPQEDYVEAAVKQSLQVHLSGAPGDILIFMPGQEDIEVTSDQIVEHLeelen 734
Cdd:TIGR01970 159 ERLSSLLPDAPVVESEGRSFPVEIRYLPLRGDQRLEDAVSRAVEHALASETGSILVFLPGQAEIRRVQEQLAERL----- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 735 APALAVLPIYSQLPSDLQAKIFQKAPDGVRKCIVATNIAETSLTVDGIMFVIDSGYCKLKVFNPRIGMDALQIYPISQAN 814
Cdd:TIGR01970 234 DSDVLICPLYGELSLAAQDRAIKPDPQGRRKVVLATNIAETSLTIEGIRVVIDSGLARVARFDPKTGITRLETVRISQAS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 815 ANQRSGRAGRTGPGQCFRLYTQSAYKnELLTTTVPEIQRTNLANVVLLLKSLGVQDLLQFHFMDPPPEDNMLNSMYQLWI 894
Cdd:TIGR01970 314 ATQRAGRAGRLEPGVCYRLWSEEQHQ-RLPAQDEPEILQADLSGLALELAQWGAKDPSDLRWLDAPPSVALAAARQLLQR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1034596784 895 LGALDNTGGLTSTGRLMVEFPLDPALSKMLIVSCDMGCSSEILLIVSMLSVPAI 948
Cdd:TIGR01970 393 LGALDAQGRLTAHGKAMAALGCHPRLAAMLLSAHSTGLAALACDLAALLEERGL 446
|
|
| DEXHc_DHX8 |
cd17971 |
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as ... |
492-670 |
4.16e-95 |
|
DEXH-box helicase domain of DEAH-box helicase 8; DEAH-box helicase 8 (DHX8 ,also known as pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22) acts late in the splicing of pre-mRNA and mediates the release of the spliced mRNA from spliceosomes. DHX8 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350729 [Multi-domain] Cd Length: 179 Bit Score: 301.32 E-value: 4.16e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 492 EQRQYLPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGGNLG 571
Cdd:cd17971 1 EQRESLPIYKLKEQLIQAVHDNQILVVIGETGSGKTTQITQYLAEAGYTSRGKIGCTQPRRVAAMSVAKRVAEEFGCCLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 572 EEVGYAIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLIVTSAT 651
Cdd:cd17971 81 QEVGYTIRFEDCTSPETVIKYMTDGMLLRECLIDPDLSQYSVIMLDEAHERTIHTDVLFGLLKKTVQKRPDLKLIVTSAT 160
|
170
....*....|....*....
gi 1034596784 652 MDAEKFAAFFGNVPIFHIP 670
Cdd:cd17971 161 LDAVKFSQYFYEAPIFTIP 179
|
|
| DEXHc_RHA-like |
cd17917 |
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ... |
513-669 |
1.64e-89 |
|
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438707 [Multi-domain] Cd Length: 159 Bit Score: 285.12 E-value: 1.64e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 513 NSIVIVVGETGSGKTTQLTQYLHEDGYT--DYGMIGCTQPRRVAAMSVAKRVSEEMGGNLGEEVGYAIRFEDCTSENTLI 590
Cdd:cd17917 1 NQVVVIVGETGSGKTTQVPQFLLEDGLAkgGKGRIVCTQPRRIAAISVAERVAEERGEKLGEEVGYQIRFESKTSSKTRI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034596784 591 KYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLIVTSATMDAEKFAAFFGNVPIFHI 669
Cdd:cd17917 81 KFCTDGILLRELLSDPLLSGYSHVILDEAHERSLDTDFLLGLLKDLLRKRPDLKVILMSATLDAEKFSSYFGGAPVIHI 159
|
|
| PRK11664 |
PRK11664 |
ATP-dependent RNA helicase HrpB; Provisional |
497-925 |
8.07e-89 |
|
ATP-dependent RNA helicase HrpB; Provisional
Pssm-ID: 236950 [Multi-domain] Cd Length: 812 Bit Score: 305.31 E-value: 8.07e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLT-QYLHEDGYTdyGMIGCTQPRRVAAMSVAKRVSEEMGGNLGEEVG 575
Cdd:PRK11664 4 LPVAAVLPELLTALKTAPQVLLKAPTGAGKSTWLPlQLLQHGGIN--GKIIMLEPRRLAARNVAQRLAEQLGEKPGETVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 576 YAIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREV-VARRSDLKLIVTSATMDA 654
Cdd:PRK11664 82 YRMRAESKVGPNTRLEVVTEGILTRMIQRDPELSGVGLVILDEFHERSLQADLALALLLDVqQGLRDDLKLLIMSATLDN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 655 EKFAAFFGNVPIFHIPGRTFPVDILFSKTPQEDYVEAAVKQSLQVHLSGAPGDILIFMPGQEDIEvtsdQIVEHLEELEN 734
Cdd:PRK11664 162 DRLQQLLPDAPVIVSEGRSFPVERRYQPLPAHQRFDEAVARATAELLRQESGSLLLFLPGVGEIQ----RVQEQLASRVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 735 APALaVLPIYSQLPSDLQAKIFQKAPDGVRKCIVATNIAETSLTVDGIMFVIDSGYCKLKVFNPRIGMDALQIYPISQAN 814
Cdd:PRK11664 238 SDVL-LCPLYGALSLAEQQKAILPAPAGRRKVVLATNIAETSLTIEGIRLVVDSGLERVARFDPKTGLTRLVTQRISQAS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 815 ANQRSGRAGRTGPGQCFRLYTQSAYKNELLTTTvPEIQRTNLANVVLLLKSLGVQDLLQFHFMDPPPEDNMLNSMYQLWI 894
Cdd:PRK11664 317 MTQRAGRAGRLEPGICLHLYSKEQAERAAAQSE-PEILHSDLSGLLLELLQWGCHDPAQLSWLDQPPAAALAAAKRLLQQ 395
|
410 420 430
....*....|....*....|....*....|.
gi 1034596784 895 LGALDNTGGLTSTGRLMVEFPLDPALSKMLI 925
Cdd:PRK11664 396 LGALDGQGRLTARGRKMAALGNDPRLAAMLV 426
|
|
| DEXHc_DHX16 |
cd17974 |
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably ... |
497-669 |
3.59e-85 |
|
DEXH-box helicase domain of DEAH-box helicase 16; DEAH-box helicase 16 (DHX16) is probably involved in pre-mRNA splicing. DHX16 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350732 [Multi-domain] Cd Length: 174 Bit Score: 273.99 E-value: 3.59e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYT-DYGMIGCTQPRRVAAMSVAKRVSEEMGGNLGEEVG 575
Cdd:cd17974 1 LPVYPYRDDLLAAVKEHQVLIIVGETGSGKTTQIPQYLHEAGYTkGGGKIGCTQPRRVAAMSVAARVAEEMGVKLGNEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 576 YAIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLIVTSATMDAE 655
Cdd:cd17974 81 YSIRFEDCTSEKTVLKYMTDGMLLREFLTEPDLASYSVMIIDEAHERTLHTDILFGLVKDIARFRPDLKLLISSATMDAE 160
|
170
....*....|....
gi 1034596784 656 KFAAFFGNVPIFHI 669
Cdd:cd17974 161 KFSAFFDDAPIFRI 174
|
|
| DEXHc_DHX33 |
cd17978 |
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA ... |
497-669 |
4.51e-84 |
|
DEXH-box helicase domain of DEAH-box helicase 33; DEAH-box helicase 33 (DHX33) stimulates RNA polymerase I transcription of the 47S precursor rRNA. DHX33 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438710 [Multi-domain] Cd Length: 178 Bit Score: 271.15 E-value: 4.51e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGGNLGEEVGY 576
Cdd:cd17978 1 LPIYSARKRLLEELRKHDTVIIIGETGSGKTTQIPQYLYEAGFARGGMIGITQPRRVAAVSVAKRVAEEMGVELGQLVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 577 AIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARR-----SDLKLIVTSAT 651
Cdd:cd17978 81 SVRFDDVTSEETRIKYMTDGMLLREAIGDPLLSKYSVIILDEAHERTVHTDVLFGLVKSAQRRRkeqklSPLKVIIMSAT 160
|
170
....*....|....*...
gi 1034596784 652 MDAEKFAAFFGNVPIFHI 669
Cdd:cd17978 161 LDADLFSEYFNGAPVLYI 178
|
|
| DEXHc_DHX15 |
cd17973 |
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA ... |
490-669 |
3.85e-83 |
|
DEXH-box helicase domain of DEAH-box helicase 15; DEAH-box helicase 15 (DHX15) is a pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. DHX15 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438709 [Multi-domain] Cd Length: 187 Bit Score: 268.90 E-value: 3.85e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 490 ILEQRQYLPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYTDYG--MIGCTQPRRVAAMSVAKRVSEEMG 567
Cdd:cd17973 6 ILEKRRELPVWEQKEDFLKLLKNNQILVLVGETGSGKTTQIPQFVLDDELPHQPkkLVACTQPRRVAAMSVAQRVAEEMD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 568 GNLGEEVGYAIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLIV 647
Cdd:cd17973 86 VKLGEEVGYSIRFEDCSSAKTILKYMTDGMLLREAMSDPLLSRYSVIILDEAHERTLATDILMGLLKEVVRRRPDLKLIV 165
|
170 180
....*....|....*....|..
gi 1034596784 648 TSATMDAEKFAAFFGNVPIFHI 669
Cdd:cd17973 166 MSATLDAGKFQKYFDNAPLLKV 187
|
|
| SF2_C_RHA |
cd18791 |
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A ... |
674-834 |
3.43e-74 |
|
C-terminal helicase domain of the RNA helicase A (RHA) family helicases; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family members are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350178 [Multi-domain] Cd Length: 171 Bit Score: 243.21 E-value: 3.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 674 FPVDILFSKTP-----------QEDYVEAAVKQSLQVHLSGAPGDILIFMPGQEDIEVTSDQIVEHLEELENAPaLAVLP 742
Cdd:cd18791 1 FPVEVYYLEDIlellgissekeDPDYVDAAVRLILQIHRTEEPGDILVFLPGQEEIERLCELLREELLSPDLGK-LLVLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 743 IYSQLPSDLQAKIFQKAPDGVRKCIVATNIAETSLTVDGIMFVIDSGYCKLKVFNPRIGMDALQIYPISQANANQRSGRA 822
Cdd:cd18791 80 LHSSLPPEEQQRVFEPPPPGVRKVVLATNIAETSITIPGVVYVIDSGLVKEKVYDPRTGLSSLVTVWISKASAEQRAGRA 159
|
170
....*....|..
gi 1034596784 823 GRTGPGQCFRLY 834
Cdd:cd18791 160 GRTRPGKCYRLY 171
|
|
| DEXHc_DHX40 |
cd17984 |
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the ... |
497-669 |
1.11e-72 |
|
DEXH-box helicase domain of DEAH-box helicase 40; DEAH-box helicase 40 (DHX40) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350742 [Multi-domain] Cd Length: 178 Bit Score: 239.37 E-value: 1.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGGNLGEEVGY 576
Cdd:cd17984 1 LPIQKQRKKLVQAVRDNSFLIVTGNTGSGKTTQLPKYLYEAGFSQHGMIGVTQPRRVAAISVAQRVAEEMKCTLGSKVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 577 AIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVV-----ARRSDLKLIVTSAT 651
Cdd:cd17984 81 QVRFDDCSSKETAIKYMTDGCLLRHILADPNLTKYSVIILDEAHERSLTTDILFGLLKKLFqekspNRKEHLKVVVMSAT 160
|
170
....*....|....*...
gi 1034596784 652 MDAEKFAAFFGNVPIFHI 669
Cdd:cd17984 161 LELAKLSAFFGNCPVFDI 178
|
|
| DEXHc_DHX35 |
cd17980 |
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and ... |
497-661 |
5.25e-68 |
|
DEXH-box helicase domain of DEAH-box helicase 35; DHX35 plays a role in colorectal cancers and seems to be associated with risk to thyroid cancers. It also has been shown to positively regulate poxviruses, such as Myxoma virus. DEAH-box helicase 35 (DHX35) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350738 [Multi-domain] Cd Length: 185 Bit Score: 226.58 E-value: 5.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYTDYG-MIGCTQPRRVAAMSVAKRVSEEMGGNLGEEVG 575
Cdd:cd17980 1 LPVFKLRNHILYLVENYQTIVIVGETGCGKSTQIPQYLAEAGWTAGGrVVGCTQPRRVAAVTVAGRVAEEMGAVLGHEVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 576 YAIRFEDCTSE-NTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLIVTSATMDA 654
Cdd:cd17980 81 YCIRFDDCTDPqATRIKFLTDGMLVREMMLDPLLTKYSVIMLDEAHERTLYTDILIGLLKKIQKKRGDLRLIVASATLDA 160
|
....*..
gi 1034596784 655 EKFAAFF 661
Cdd:cd17980 161 EKFRDFF 167
|
|
| DEXHc_HrpA |
cd17989 |
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA ... |
497-669 |
8.50e-67 |
|
DEXH-box helicase domain of ATP-dependent RNA helicase HrpA; HrpA is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpA belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350747 [Multi-domain] Cd Length: 173 Bit Score: 222.33 E-value: 8.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGGNLGEEVGY 576
Cdd:cd17989 1 LPVSQKRDEIAKAIAENQVVIIAGETGSGKTTQLPKICLELGRGIRGLIGHTQPRRLAARSVAERIAEELKTELGGAVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 577 AIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLIVTSATMDAEK 656
Cdd:cd17989 81 KVRFTDQTSDETCVKLMTDGILLAETQTDRYLRAYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATIDAER 160
|
170
....*....|...
gi 1034596784 657 FAAFFGNVPIFHI 669
Cdd:cd17989 161 FSRHFNNAPIIEV 173
|
|
| DEXHc_DHX37 |
cd17982 |
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the ... |
497-657 |
4.12e-65 |
|
DEXH-box helicase domain of DEAH-box helicase 37; DHX37 plays a role in the development of the human nervous system and has been linked to schizophrenia. It also negatively regulates poxviruses such as Myxoma virus. DEAH-box helicase 37 (DHX37) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350740 [Multi-domain] Cd Length: 191 Bit Score: 218.38 E-value: 4.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYTDY-----GMIGCTQPRRVAAMSVAKRVSEEMGGnLG 571
Cdd:cd17982 1 LPILAEEQEIMEAINENPVVIICGETGSGKTTQVPQFLYEAGFGSPesdnpGMIGITQPRRVAAVSMAKRVAEELNV-FG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 572 EEVGYAIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSD--------- 642
Cdd:cd17982 80 KEVSYQIRYDSTVSENTKIKFMTDGVLLKEIQTDFLLRKYSVIIIDEAHERSVNTDILIGMLSRIVPLRAKlylqdqtvk 159
|
170
....*....|....*.
gi 1034596784 643 -LKLIVTSATMDAEKF 657
Cdd:cd17982 160 pLKLVIMSATLRVEDF 175
|
|
| DEXHc_DHX34 |
cd17979 |
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in ... |
497-669 |
3.64e-53 |
|
DEXH-box helicase domain of DEAH-box helicase 34; DEAH-box helicase 34 (DHX34) plays a role in the nonsense-mediated decay (NMD), a surveillance mechanism that degrades aberrant mRNAs. DHX34 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350737 [Multi-domain] Cd Length: 170 Bit Score: 183.41 E-value: 3.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYTDygmIGCTQPRRVAAMSVAKRVSEEMGGNLGEEVGY 576
Cdd:cd17979 1 LPIAQYREKIIELLKTHQVVIVAGDTGCGKSTQVPQYLLAAGFRH---IACTQPRRIACISLAKRVAFESLNQYGSKVAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 577 AIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLIVTSATMDAEK 656
Cdd:cd17979 78 QIRFERTRTLATKLLFLTEGLLLRQIQRDASLPQYNVLILDEVHERHLHGDFLLGVLRCLLRLRPDLKLILMSATINIEL 157
|
170
....*....|...
gi 1034596784 657 FAAFFGNVPIFHI 669
Cdd:cd17979 158 FSGYFEGAPVVQV 170
|
|
| DEXHc_YTHDC2 |
cd17987 |
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) ... |
497-669 |
3.30e-49 |
|
DEXH-box helicase domain of YTH domain containing 2; YTH domain containing 2 (YTHDC2) regulates mRNA translation and stability via binding to N6-methyladenosine, a modified RNA nucleotide enriched in the stop codons and 3' UTRs of eukaryotic messenger RNAs. YTHDC2 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350745 [Multi-domain] Cd Length: 176 Bit Score: 172.32 E-value: 3.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYTDYG--MIGCTQPRRVAAMSVAKRVSEEMGGNLGEEV 574
Cdd:cd17987 1 LPVFEKQEQIVRIIKENKVVLIVGETGSGKTTQIPQFLLDDCYANGIpcRIFCTQPRRLAAIAVAERVAAERGEKIGQTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 575 GYAIRFEDCTSENTLIKYMTDGILLRESL-READLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLIVTSATMD 653
Cdd:cd17987 81 GYQIRLESRVSPKTLLTFCTNGVLLRTLMaGDSALSTVTHVIVDEVHERDRFSDFLLTKLRDILQKHPNLKLILSSAALD 160
|
170
....*....|....*.
gi 1034596784 654 AEKFAAFFGNVPIFHI 669
Cdd:cd17987 161 VNLFIRYFGSCPVIYI 176
|
|
| DEXHc_DHX29 |
cd17975 |
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of ... |
497-669 |
2.28e-48 |
|
DEXH-box helicase domain of DEAH-box helicase 29; DEAH-box helicase 29 (DHX29) is a part of the 43S pre-initiation complex involved in translation initiation of mRNAs with structured 5'-UTRs. DHX29 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350733 [Multi-domain] Cd Length: 183 Bit Score: 170.48 E-value: 2.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYTDYGM-----IGCTQPRRVAAMSVAKRVSEEMG---- 567
Cdd:cd17975 1 LPVFKHRESILETLKRHRVVVVAGETGSGKSTQVPQFLLEDLLLNGGTaqkcnIVCTQPRRISAMSLATRVCEELGcesg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 568 -GNLGEEVGYAIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLI 646
Cdd:cd17975 81 pGGKNSLCGYQIRMESRTGEATRLLYCTTGVLLRKLQEDGLLSSISHIIVDEVHERSVQSDFLLIILKEILHKRSDLHLI 160
|
170 180
....*....|....*....|...
gi 1034596784 647 VTSATMDAEKFAAFFGNVPIFHI 669
Cdd:cd17975 161 LMSATVDCEKFSSYFTHCPILRI 183
|
|
| DEXHc_DHX36 |
cd17981 |
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as ... |
497-669 |
2.92e-47 |
|
DEXH-box helicase domain of DEAH-box helicase 36; DEAH-box helicase 36 (DHX36, also known as G4-resolvase 1 or G4R1, MLE-like protein 1 and RNA helicase associated with AU-rich element or RHAU) unwinds a G4-quadruplex in human telomerase RNA. DHX36 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350739 [Multi-domain] Cd Length: 180 Bit Score: 166.94 E-value: 2.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHED----GYTDYGMIGCTQPRRVAAMSVAKRVSEEMGGN--L 570
Cdd:cd17981 1 LPSYGMKQEIINMIDNNQVTVISGETGCGKTTQVTQFILDDaierGKGSSCRIVCTQPRRISAISVAERVAAERAEScgL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 571 GEEVGYAIRFED-CTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLIVTS 649
Cdd:cd17981 81 GNSTGYQIRLESrKPRKQGSILYCTTGIVLQWLQSDPHLSNVSHLVLDEIHERNLQSDVLMGIVKDLLPFRSDLKVILMS 160
|
170 180
....*....|....*....|
gi 1034596784 650 ATMDAEKFAAFFGNVPIFHI 669
Cdd:cd17981 161 ATLNAEKFSDYFNNCPMIHI 180
|
|
| DEXHc_HrpB |
cd17990 |
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ... |
497-667 |
1.59e-45 |
|
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438711 [Multi-domain] Cd Length: 174 Bit Score: 161.73 E-value: 1.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLT-QYLHEDGYTDyGMIGCTQPRRVAAMSVAKRVSEEMGGNLGEEVG 575
Cdd:cd17990 1 LPIAAVLPALRAALDAGGQVVLEAPPGAGKTTRVPlALLAELWIAG-GKIIVLEPRRVAARAAARRLATLLGEAPGETVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 576 YAIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVV-ARRSDLKLIVTSATMDA 654
Cdd:cd17990 80 YRVRGESRVGRRTRVEVVTEGVLLRRLQRDPELSGVGAVILDEFHERSLDADLALALLLEVQqLLRDDLRLLAMSATLDG 159
|
170
....*....|...
gi 1034596784 655 EKFAAFFGNVPIF 667
Cdd:cd17990 160 DGLAALLPEAPVV 172
|
|
| DEXHc_DHX9 |
cd17972 |
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ... |
488-669 |
6.40e-45 |
|
DEXH-box helicase domain of DEAH-box helicase 9; DEAH-box helicase 9 (DHX9, also known as ATP-dependent RNA helicase A or RHA and leukophysin or LKP) plays an important role in many cellular processes, including regulation of DNA replication, transcription, translation, microRNA biogenesis, RNA processing and transport, and maintenance of genomic stability. DHX9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350730 [Multi-domain] Cd Length: 234 Bit Score: 162.31 E-value: 6.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 488 KSILEQRQYLPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHED----GYTDYGMIGCTQPRRVAAMSVAKRVS 563
Cdd:cd17972 50 QQILQERELLPVKKFREEILEAISNNPVVIIRGATGCGKTTQVPQYILDDfiqnDRAAECNIVVTQPRRISAVSVAERVA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 564 EEMGGNLGEEVGYAIRFEDCTSE-NTLIKYMTDGILLREslREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSD 642
Cdd:cd17972 130 FERGEEVGKSCGYSVRFESVLPRpHASILFCTVGVLLRK--LEAGIRGISHVIVDEIHERDINTDFLLVVLRDVVQAYPD 207
|
170 180
....*....|....*....|....*..
gi 1034596784 643 LKLIVTSATMDAEKFAAFFGNVPIFHI 669
Cdd:cd17972 208 LRVILMSATIDTSMFCEYFFNCPVIEV 234
|
|
| DEXHc_DHX32 |
cd17977 |
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the ... |
497-666 |
6.15e-42 |
|
DEXH-box helicase domain of DEAH-box helicase 32; DEAH-box helicase 32 (DHX32) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350735 [Multi-domain] Cd Length: 176 Bit Score: 151.52 E-value: 6.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHE---DGYTDYGMIGCTQPRRVAAMSVAKRVSEEMGGNLGEE 573
Cdd:cd17977 1 LPVWEAKYEFMESLAHNQIVIVSGDAKTGKSSQIPQWCAEyclSAHYQHGVVVCTQVHKQTAVWLALRVADEMDVNIGHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 574 VGYAIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLIVTSATMD 653
Cdd:cd17977 81 VGYVIPFENCCTNETILRYCTDDMLLREMMSDPLLESYGVIILDDAHERTVSTDVLLGLLKDVLLSRPELKLVIITCPHL 160
|
170
....*....|...
gi 1034596784 654 AEKFAAFFGNVPI 666
Cdd:cd17977 161 SSKLLSYYGNVPL 173
|
|
| DEXHc_DHX57 |
cd17985 |
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the ... |
497-669 |
2.53e-41 |
|
DEXH-box helicase domain of DEAH-box helicase 57; DEAH-box helicase 57 (DHX57) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350743 [Multi-domain] Cd Length: 177 Bit Score: 149.99 E-value: 2.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHED----GYTDYGMIGCTQPRRVAAMSVAKRVSEEMGGNLGE 572
Cdd:cd17985 1 LPAWQERETILELLEKHQVLVISGMTGCGKTTQIPQFILDNslqgPPLPVANIICTQPRRISAISVAERVAQERAERVGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 573 EVGYAIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLIVTSATM 652
Cdd:cd17985 81 SVGYQIRLESVKSSATRLLYCTTGVLLRRLEGDPTLQGVTHVIVDEVHERTEESDFLLLVLKDLMVQRPDLKVILMSATL 160
|
170
....*....|....*..
gi 1034596784 653 DAEKFAAFFGNVPIFHI 669
Cdd:cd17985 161 NAELFSDYFNSCPVIHI 177
|
|
| DEXHc_DHX30 |
cd17976 |
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an ... |
497-669 |
8.51e-41 |
|
DEXH-box helicase domain of DEAH-box helicase 30; DEAH-box helicase 30 (DHX30) plays an important role in the assembly of the mitochondrial large ribosomal subunit. DHX30 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350734 [Multi-domain] Cd Length: 178 Bit Score: 148.40 E-value: 8.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGC----TQPRRVAAMSVAKRVSEEMGGNLGE 572
Cdd:cd17976 1 LPVDSHKESILSAIEQNPVVVISGDTGCGKTTRIPQFILEDYVLRGRGARCnvviTQPRRISAVSVAQRVAHELGPNLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 573 EVGYAIRFEDCTSENT-LIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLIVTSAT 651
Cdd:cd17976 81 NVGYQVRLESRPPPRGgALLFCTVGVLLKKLQSNPRLEGVSHVIVDEVHERDVNTDFLLILLKGVLQLNPELRVVLMSAT 160
|
170
....*....|....*...
gi 1034596784 652 MDAEKFAAFFGNVPIFHI 669
Cdd:cd17976 161 GDNQRLSRYFGGCPVVRV 178
|
|
| DEXHc_TDRD9 |
cd17988 |
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also ... |
497-662 |
1.20e-40 |
|
DEXH-box helicase domain of tudor domain containing 9; Tudor domain containing 9 (TDRD9, also known as HIG-1or NET54 or C14orf75) is a part of the nuclear PIWI-interacting RNA (piRNA) pathway essential for transposon silencing and male fertility TDRD9 belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350746 [Multi-domain] Cd Length: 180 Bit Score: 148.03 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNSIVIVVGETGSGKTTQLTQYLHEDGYTD--YGMIGCTQPRRVAAMSVAKRVSEEMGGNLGEEV 574
Cdd:cd17988 1 LPIYAKREEILSLIEANSVVIIKGATGCGKTTQLPQFILDHYYKRgkYCNIVVTQPRRIAAISIARRVSQEREWTLGSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 575 GYAIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSD-LKLIVTSATMD 653
Cdd:cd17988 81 GYQVGLERPASEETRLIYCTTGVLLQKLINNKTLTEYTHIILDEVHERDQELDFLLLVVRRLLRTNSRhVKIILMSATIS 160
|
....*....
gi 1034596784 654 AEKFAAFFG 662
Cdd:cd17988 161 CKEFADYFT 169
|
|
| DEXQc_DQX1 |
cd17986 |
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 ... |
497-669 |
4.87e-40 |
|
DEXQ-box helicase domain of DEAQ-box RNA dependent ATPase 1; DEAQ-box RNA dependent ATPase 1 (DQX1) belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350744 [Multi-domain] Cd Length: 177 Bit Score: 146.20 E-value: 4.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 497 LPIFAVQQELLTIIRDNS-IVIVVGETGSGKTTQLTQYLHEDGYT---DYGMIGCTQPRRVAAMSVAKRVSEEMGGNLGE 572
Cdd:cd17986 1 LPIWAAKFTFLEQLESPSgIVLVSGEPGSGKSTQVPQWCAEFALSrgfQKGQVTVTQPHPLAARSLALRVADEMDLNLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 573 EVGYAIRFEDCTSENTLIKYMTDGILLRESLREADLDHYSAIIMDEAHERSLNTDVLFGLLREVVARRSDLKLIVTSATM 652
Cdd:cd17986 81 EVGYSIPQEDCTGPNTILRFCWDRLLLQEMTSTPLLGAWGVVVLDEAQERSVASDSLLGLLKDVRLQRPELRVVVVTSPA 160
|
170
....*....|....*..
gi 1034596784 653 DAEKFAAFFGNVPIFHI 669
Cdd:cd17986 161 LEPKLRAFWGNPPVVHV 177
|
|
| HA2 |
smart00847 |
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino ... |
895-977 |
2.72e-30 |
|
Helicase associated domain (HA2) Add an annotation; This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.
Pssm-ID: 214852 [Multi-domain] Cd Length: 82 Bit Score: 114.67 E-value: 2.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 895 LGALDNTGGLTSTGRLMVEFPLDPALSKMLIVSCDMGCSSEILLIVSMLSVPAifYRPKGREEESDQIREKFAVPESDHL 974
Cdd:smart00847 2 LGALDDDGRLTPLGRKMAELPLDPRLAKMLLAAAEFGCLDEILTIVAMLSVGD--PRPKEKREDADAARRRFADPESDHL 79
|
...
gi 1034596784 975 TYL 977
Cdd:smart00847 80 TLL 82
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
491-678 |
6.62e-30 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 117.98 E-value: 6.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 491 LEQRQYLPIFAVQQELL-TIIRDNSIVIVVGETGSGKTTQLTQYLHEDGY-TDYGMIGCTQPRRVAAMSVAKRVSEEMGG 568
Cdd:smart00487 1 IEKFGFEPLRPYQKEAIeALLSGLRDVILAAPTGSGKTLAALLPALEALKrGKGGRVLVLVPTRELAEQWAEELKKLGPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 569 NLGEEVGY------AIRFEDCTSENTLIKYMTDGILLRESLREA-DLDHYSAIIMDEAHERS--LNTDVLFGLLREVvar 639
Cdd:smart00487 81 LGLKVVGLyggdskREQLRKLESGKTDILVTTPGRLLDLLENDKlSLSNVDLVILDEAHRLLdgGFGDQLEKLLKLL--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1034596784 640 RSDLKLIVTSATM--DAEKFAAFFGNVPIFHIPGRTFPVDI 678
Cdd:smart00487 158 PKNVQLLLLSATPpeEIENLLELFLNDPVFIDVGFTPLEPI 198
|
|
| HA2 |
pfam04408 |
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in ... |
891-976 |
4.68e-26 |
|
Helicase associated domain (HA2); This presumed domain is about 90 amino acid residues in length. It is found is a diverse set of RNA helicases. Its function is unknown, however it seems likely to be involved in nucleic acid binding.
Pssm-ID: 461295 [Multi-domain] Cd Length: 104 Bit Score: 103.47 E-value: 4.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 891 QLWILGALDNTGGLTSTGRLMVEFPLDPALSKMLIVSCDMGCSSEILLIVSMLSVPAIFYRP-------------KGREE 957
Cdd:pfam04408 4 LLYYLGALDEDGELTPLGRKMAELPLDPRLAKMLLAAAELGCLDEVLTIVAALSVRDPFVQPnfldprsaakaarRRRRA 83
|
90 100
....*....|....*....|.
gi 1034596784 958 ESDQIREKFAVP--ESDHLTY 976
Cdd:pfam04408 84 ADEKARAKFARLdlEGDHLTL 104
|
|
| OB_NTP_bind |
pfam07717 |
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus ... |
1034-1111 |
2.27e-20 |
|
Oligonucleotide/oligosaccharide-binding (OB)-fold; This family is found towards the C-terminus of the DEAD-box helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. There do seem to be a couple of instances where it occurs by itself -. The structure PDB:3i4u adopts an OB-fold. helicases (pfam00270). In these helicases it is apparently always found in association with pfam04408. This C-terminal domain of the yeast helicase contains an oligonucleotide/oligosaccharide-binding (OB)-fold which seems to be placed at the entrance of the putative nucleic acid cavity. It also constitutes the binding site for the G-patch-containing domain of Pfa1p. When found on DEAH/RHA helicases, this domain is central to the regulation of the helicase activity through its binding of both RNA and G-patch domain proteins.
Pssm-ID: 400182 [Multi-domain] Cd Length: 82 Bit Score: 86.54 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 1034 VRKCICAAYFHQAAKLKGIG-EYVNIRTGMPCHLHPTSSLF-GMGYTPDYIVYHELVMTTKEYMQCVTAVDGEWLAELGP 1111
Cdd:pfam07717 1 LRAALAAGLYPNVARRDPKGkGYTTLSDNQRVFIHPSSVLFnEKTFPPEWVVYQELVETTKVYIRTVTAISPEWLLLFAP 80
|
|
| PHA02653 |
PHA02653 |
RNA helicase NPH-II; Provisional |
502-835 |
7.66e-18 |
|
RNA helicase NPH-II; Provisional
Pssm-ID: 177443 [Multi-domain] Cd Length: 675 Bit Score: 88.88 E-value: 7.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 502 VQQELLTIIRDNSIVIVVGETGSGKTTQLTQ------YLHeDGYTDYGMIGCTQPRRVAAMSVAkRVS--EEMGGNLGEE 573
Cdd:PHA02653 168 VQLKIFEAWISRKPVVLTGGTGVGKTSQVPKlllwfnYLF-GGFDNLDKIDPNFIERPIVLSLP-RVAlvRLHSITLLKS 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 574 VGY--------AIRFEDCTSE--NTLIKymTDGILL---RESLreADLDHYSAIIMDEAHERSLNTDVLFGLLREVVAR- 639
Cdd:PHA02653 246 LGFdeidgspiSLKYGSIPDEliNTNPK--PYGLVFsthKLTL--NKLFDYGTVIIDEVHEHDQIGDIIIAVARKHIDKi 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 640 RSdlkLIVTSATM--DAEKFAAFFGNVPIFHIPGRT-FPVDILFSKTPQE-----DYVEAAVK---QSLQVHLSGAPGDI 708
Cdd:PHA02653 322 RS---LFLMTATLedDRDRIKEFFPNPAFVHIPGGTlFPISEVYVKNKYNpknkrAYIEEEKKnivTALKKYTPPKGSSG 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 709 LIFMPGQEDIEvtsdQIVEHLEELEnaPALAVLPIYSQLPS--DLQAKIFQKAPDGVrkcIVATNIAETSLTVDGIMFVI 786
Cdd:PHA02653 399 IVFVASVSQCE----EYKKYLEKRL--PIYDFYIIHGKVPNidEILEKVYSSKNPSI---IISTPYLESSVTIRNATHVY 469
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1034596784 787 DSGycklKVFNPR-IGMDalQIYpISQANANQRSGRAGRTGPGQCFRLYT 835
Cdd:PHA02653 470 DTG----RVYVPEpFGGK--EMF-ISKSMRTQRKGRVGRVSPGTYVYFYD 512
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
723-826 |
2.28e-14 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 69.16 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 723 DQIVEHLEELEnapaLAVLPIYSQLPSDLQAKIFQKAPDGVRKCIVATNIAETSLTVDGIMFVIDSGycklkvfnprigm 802
Cdd:smart00490 1 EELAELLKELG----IKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYD------------- 63
|
90 100
....*....|....*....|....
gi 1034596784 803 dalqiYPISQANANQRSGRAGRTG 826
Cdd:smart00490 64 -----LPWSPASYIQRIGRAGRAG 82
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
697-826 |
1.19e-12 |
|
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: 65.31 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 697 LQVHLSGAPGDILIFMPGQEDIEVtsdqivEHLEELENAPalaVLPIYSQLPSDLQAKIFQKAPDGVRKCIVATNIAETS 776
Cdd:pfam00271 7 LELLKKERGGKVLIFSQTKKTLEA------ELLLEKEGIK---VARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERG 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1034596784 777 LTVDGIMFVIDSGYCklkvFNPrigmdalqiypisqANANQRSGRAGRTG 826
Cdd:pfam00271 78 LDLPDVDLVINYDLP----WNP--------------ASYIQRIGRAGRAG 109
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
516-651 |
2.85e-07 |
|
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: 51.25 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 516 VIVVGETGSGKTTQLTQYLHEDGYtdygmigcTQPRRVAAMSVAKRVSEEMGGNLGEEVGYAIRFEDCTSENTL------ 589
Cdd:cd00046 4 VLITAPTGSGKTLAALLAALLLLL--------KKGKKVLVLVPTKALALQTAERLRELFGPGIRVAVLVGGSSAeerekn 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034596784 590 ------IKYMTDGILLRESLREA--DLDHYSAIIMDEAHERSLNTDVLF-GLLREVVARRSDLKLIVTSAT 651
Cdd:cd00046 76 klgdadIIIATPDMLLNLLLREDrlFLKDLKLIIVDEAHALLIDSRGALiLDLAVRKAGLKNAQVILLSAT 146
|
|
| DEXHc_viral_Ns3 |
cd17931 |
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ... |
522-620 |
2.55e-05 |
|
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350689 [Multi-domain] Cd Length: 151 Bit Score: 45.62 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 522 TGSGKTTQLTQYLHEDGYTDYGMIGCTQPRRVAAMSVAKRVSeemggnlGEEVGY---AIRFEDctSENTLIKYMTDGIL 598
Cdd:cd17931 10 PGAGKTTRVLPQIIREAIKKRLRTLVLAPTRVVAAEMYEALR-------GLPIRYrtgAVKEEH--GGNEIVDYMCHGTF 80
|
90 100
....*....|....*....|..
gi 1034596784 599 LRESLREADLDHYSAIIMDEAH 620
Cdd:cd17931 81 TCRLLSPKRVPNYNLIIMDEAH 102
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
514-647 |
1.27e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 43.10 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 514 SIVIVVGETGSGKTTQLTQYLHEDGYTDYGMIGCTqprrVAAMSVAKRVSEEMGGNLGEEVGYAIRFEDCTSentlikym 593
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVD----LPSGTSPKDLLRALLRALGLPLSGRLSKEELLA-------- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1034596784 594 tdgiLLRESLREADLDHysAIIMDEAHerSLNTDVLFGLLREVVARRSDLKLIV 647
Cdd:pfam13401 74 ----ALQQLLLALAVAV--VLIIDEAQ--HLSLEALEELRDLLNLSSKLLQLIL 119
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
352-660 |
1.72e-04 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 45.95 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 352 VVHRLEVDEDFEEDNAAKVHLMVHNLVPPFLDGRIVFTKQPEPVIPVKDATSDLAIIARKGSQTVRKHREQKERKKAQHK 431
Cdd:COG5635 19 DLLVTRLAIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALSALLLVLLLLESLLLLLLLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 432 HWELAGTKLGDIMGVKKEEEPDKAVTEDGKVDYRTEQKFADHMKRKSEASSEFAKKKSILEQRQYLPIFAVQQELLTIIR 511
Cdd:COG5635 99 LLAEALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLERIESLKRLELLEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 512 DNSIVIVVGETGSGKTTqLTQYLhedgytdygmigctqprrvaAMSVAKRvseemggNLGEEVGYAIRFE--DCTSENTL 589
Cdd:COG5635 179 KKKRLLILGEPGSGKTT-LLRYL--------------------ALELAER-------YLDAEDPIPILIElrDLAEEASL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 590 IKYMTDGILLRESLREAD----LDHYSAIIM----DEAHERSLNTDVLfGLLREVVARRSDLKLIVTS--ATMDAEKFAA 659
Cdd:COG5635 231 EDLLAEALEKRGGEPEDAlerlLRNGRLLLLldglDEVPDEADRDEVL-NQLRRFLERYPKARVIITSrpEGYDSSELEG 309
|
.
gi 1034596784 660 F 660
Cdd:COG5635 310 F 310
|
|
| DEXHc_dicer |
cd18034 |
DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded ... |
503-620 |
2.66e-03 |
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DEXH-box helicase domain of endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicers exist throughout eukaryotes, and a subset have an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350792 [Multi-domain] Cd Length: 200 Bit Score: 40.33 E-value: 2.66e-03
10 20 30 40 50 60 70 80
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gi 1034596784 503 QQELLTI-IRDNSIVivVGETGSGKT---TQLTQYLHEDGYtdygmiGCTQPRRVAAMSV---------AKRVSE----- 564
Cdd:cd18034 7 QLELFEAaLKRNTIV--VLPTGSGKTliaVMLIKEMGELNR------KEKNPKKRAVFLVptvplvaqqAEAIRShtdlk 78
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034596784 565 --EMGGNLGEEVGYAIRFEDCTSENTLIkYMTDGILLrESLREA--DLDHYSAIIMDEAH 620
Cdd:cd18034 79 vgEYSGEMGVDKWTKERWKEELEKYDVL-VMTAQILL-DALRHGflSLSDINLLIFDECH 136
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| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
767-834 |
5.34e-03 |
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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: 36.91 E-value: 5.34e-03
10 20 30 40 50 60 70
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gi 1034596784 767 IVATNIAETSLTVDGIMFVIDSGYcklkvfnprigmdalqiyPISQANANQRSGRAGRTG--PGQCFRLY 834
Cdd:cd18785 26 LVATNVLGEGIDVPSLDTVIFFDP------------------PSSAASYIQRVGRAGRGGkdEGEVILFV 77
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