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Database: UniProt
Entry: Q96C10
LinkDB: Q96C10
Original site: Q96C10 
ID   DHX58_HUMAN             Reviewed;         678 AA.
AC   Q96C10; Q9HAM6;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   11-DEC-2019, entry version 147.
DE   RecName: Full=Probable ATP-dependent RNA helicase DHX58;
DE            EC=3.6.4.13;
DE   AltName: Full=Probable ATP-dependent helicase LGP2;
DE   AltName: Full=Protein D11Lgp2 homolog;
DE   AltName: Full=RIG-I-like receptor 3;
DE            Short=RLR-3;
DE   AltName: Full=RIG-I-like receptor LGP2;
DE            Short=RLR;
GN   Name=DHX58; Synonyms=D11LGP2E, LGP2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION.
RX   PubMed=16116171; DOI=10.4049/jimmunol.175.5.2851;
RA   Yoneyama M., Kikuchi M., Matsumoto K., Imaizumi T., Miyagishi M., Taira K.,
RA   Foy E., Loo Y.-M., Gale M. Jr., Akira S., Yonehara S., Kato A., Fujita T.;
RT   "Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and
RT   LGP2 in antiviral innate immunity.";
RL   J. Immunol. 175:2851-2858(2005).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH MAVS AND DDX58.
RX   PubMed=17020950; DOI=10.1128/jvi.01325-06;
RA   Komuro A., Horvath C.M.;
RT   "RNA- and virus-independent inhibition of antiviral signaling by RNA
RT   helicase LGP2.";
RL   J. Virol. 80:12332-12342(2006).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH DDX58.
RX   PubMed=17190814; DOI=10.1073/pnas.0606699104;
RA   Saito T., Hirai R., Loo Y.-M., Owen D., Johnson C.L., Sinha S.C., Akira S.,
RA   Fujita T., Gale M. Jr.;
RT   "Regulation of innate antiviral defenses through a shared repressor domain
RT   in RIG-I and LGP2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:582-587(2007).
RN   [6]
RP   INTERACTION WITH ATG5 AND ATG12.
RX   PubMed=17709747; DOI=10.1073/pnas.0704014104;
RA   Jounai N., Takeshita F., Kobiyama K., Sawano A., Miyawaki A., Xin K.Q.,
RA   Ishii K.J., Kawai T., Akira S., Suzuki K., Okuda K.;
RT   "The Atg5-Atg12 conjugate associates with innate antiviral immune
RT   responses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:14050-14055(2007).
RN   [7]
RP   REVIEW ON FUNCTION.
RX   PubMed=17473309; DOI=10.1126/stke.3842007pe20;
RA   Vitour D., Meurs E.F.;
RT   "Regulation of interferon production by RIG-I and LGP2: a lesson in self-
RT   control.";
RL   Sci. STKE 2007:PE20-PE20(2007).
RN   [8]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=18411269; DOI=10.1074/jbc.m800542200;
RA   Murali A., Li X., Ranjith-Kumar C.T., Bhardwaj K., Holzenburg A., Li P.,
RA   Kao C.C.;
RT   "Structure and function of LGP2, a DEX(D/H) helicase that regulates the
RT   innate immunity response.";
RL   J. Biol. Chem. 283:15825-15833(2008).
RN   [9]
RP   FUNCTION.
RX   PubMed=19211564; DOI=10.1074/jbc.m807365200;
RA   Bamming D., Horvath C.M.;
RT   "Regulation of signal transduction by enzymatically inactive antiviral RNA
RT   helicase proteins MDA5, RIG-I, and LGP2.";
RL   J. Biol. Chem. 284:9700-9712(2009).
RN   [10]
RP   INTERACTION WITH PARAMYXOVIRUSES NON-STRUCTURAL PROTEIN V (MICROBIAL
RP   INFECTION).
RX   PubMed=19403670; DOI=10.1128/jvi.00153-09;
RA   Parisien J.P., Bamming D., Komuro A., Ramachandran A., Rodriguez J.J.,
RA   Barber G., Wojahn R.D., Horvath C.M.;
RT   "A shared interface mediates paramyxovirus interference with antiviral RNA
RT   helicases MDA5 and LGP2.";
RL   J. Virol. 83:7252-7260(2009).
RN   [11]
RP   REVIEW ON FUNCTION.
RX   PubMed=21616437; DOI=10.1016/j.immuni.2011.05.003;
RA   Loo Y.M., Gale M. Jr.;
RT   "Immune signaling by RIG-I-like receptors.";
RL   Immunity 34:680-692(2011).
RN   [12]
RP   FUNCTION.
RX   PubMed=21187438; DOI=10.4049/jimmunol.1002862;
RA   Broquet A.H., Hirata Y., McAllister C.S., Kagnoff M.F.;
RT   "RIG-I/MDA5/MAVS are required to signal a protective IFN response in
RT   rotavirus-infected intestinal epithelium.";
RL   J. Immunol. 186:1618-1626(2011).
RN   [13]
RP   FUNCTION.
RX   PubMed=21525357; DOI=10.1128/jvi.00302-11;
RA   Chopy D., Pothlichet J., Lafage M., Megret F., Fiette L., Si-Tahar M.,
RA   Lafon M.;
RT   "Ambivalent role of the innate immune response in rabies virus
RT   pathogenesis.";
RL   J. Virol. 85:6657-6668(2011).
RN   [14]
RP   INTERACTION WITH DDX60.
RX   PubMed=21791617; DOI=10.1128/mcb.01368-10;
RA   Miyashita M., Oshiumi H., Matsumoto M., Seya T.;
RT   "DDX60, a DEXD/H box helicase, is a novel antiviral factor promoting RIG-I-
RT   like receptor-mediated signaling.";
RL   Mol. Cell. Biol. 31:3802-3819(2011).
RN   [15]
RP   REVIEW ON FUNCTION.
RX   PubMed=21481967; DOI=10.1016/j.ejcb.2011.01.011;
RA   Eisenaecher K., Krug A.;
RT   "Regulation of RLR-mediated innate immune signaling--it is all about
RT   keeping the balance.";
RL   Eur. J. Cell Biol. 91:36-47(2012).
RN   [16]
RP   REVIEW ON FUNCTION.
RX   PubMed=21496944; DOI=10.1016/j.ejcb.2011.01.015;
RA   Schmidt A., Rothenfusser S., Hopfner K.P.;
RT   "Sensing of viral nucleic acids by RIG-I: from translocation to
RT   translation.";
RL   Eur. J. Cell Biol. 91:78-85(2012).
RN   [17]
RP   INTERACTION WITH ANKRD17.
RX   PubMed=23711367; DOI=10.1016/j.febslet.2013.05.037;
RA   Menning M., Kufer T.A.;
RT   "A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and
RT   Nod2-mediated inflammatory responses.";
RL   FEBS Lett. 587:2137-2142(2013).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 541-678 IN COMPLEX WITH RNA,
RP   FUNCTION, SUBUNIT, MUTAGENESIS OF LYS-634 AND LYS-651, AND ZINC-BINDING
RP   SITES.
RX   PubMed=19278996; DOI=10.1074/jbc.m900818200;
RA   Li X., Ranjith-Kumar C.T., Brooks M.T., Dharmaiah S., Herr A.B., Kao C.,
RA   Li P.;
RT   "The RIG-I-like receptor LGP2 recognizes the termini of double-stranded
RT   RNA.";
RL   J. Biol. Chem. 284:13881-13891(2009).
RN   [19]
RP   STRUCTURE BY NMR OF 546-678, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=19380577; DOI=10.1074/jbc.m109.007179;
RA   Takahasi K., Kumeta H., Tsuduki N., Narita R., Shigemoto T., Hirai R.,
RA   Yoneyama M., Horiuchi M., Ogura K., Fujita T., Inagaki F.;
RT   "Solution structures of cytosolic RNA sensor MDA5 and LGP2 C-terminal
RT   domains: identification of the RNA recognition loop in RIG-I-like
RT   receptors.";
RL   J. Biol. Chem. 284:17465-17474(2009).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 537-678, FUNCTION, SUBUNIT,
RP   MUTAGENESIS OF LYS-634, AND ZINC-BINDING SITES.
RX   PubMed=19208642; DOI=10.1093/nar/gkp059;
RA   Pippig D.A., Hellmuth J.C., Cui S., Kirchhofer A., Lammens K., Lammens A.,
RA   Schmidt A., Rothenfusser S., Hopfner K.-P.;
RT   "The regulatory domain of the RIG-I family ATPase LGP2 senses double-
RT   stranded RNA.";
RL   Nucleic Acids Res. 37:2014-2025(2009).
CC   -!- FUNCTION: Acts as a regulator of DDX58/RIG-I and IFIH1/MDA5 mediated
CC       antiviral signaling. Cannot initiate antiviral signaling as it lacks
CC       the CARD domain required for activating MAVS/IPS1-dependent signaling
CC       events. Can have both negative and positive regulatory functions
CC       related to DDX58/RIG-I and IFIH1/MDA5 signaling and this role in
CC       regulating signaling may be complex and could probably depend on
CC       characteristics of the infecting virus or target cells, or both. Its
CC       inhibitory action on DDX58/RIG-I signaling may involve the following
CC       mechanisms: competition with DDX58/RIG-I for binding to the viral RNA,
CC       binding to DDX58/RIG-I and inhibiting its dimerization and interaction
CC       with MAVS/IPS1, competing with IKBKE in its binding to MAVS/IPS1
CC       thereby inhibiting activation of interferon regulatory factor 3 (IRF3).
CC       Its positive regulatory role may involve unwinding or stripping
CC       nucleoproteins of viral RNA thereby facilitating their recognition by
CC       DDX58/RIG-I and IFIH1/MDA5. Involved in the innate immune response to
CC       various RNA viruses and some DNA viruses such as poxviruses, and also
CC       to the bacterial pathogen Listeria monocytogenes. Can bind both ssRNA
CC       and dsRNA, with a higher affinity for dsRNA. Shows a preference to 5'-
CC       triphosphorylated RNA, although it can recognize RNA lacking a 5'-
CC       triphosphate. {ECO:0000269|PubMed:16116171,
CC       ECO:0000269|PubMed:17020950, ECO:0000269|PubMed:17190814,
CC       ECO:0000269|PubMed:18411269, ECO:0000269|PubMed:19208642,
CC       ECO:0000269|PubMed:19211564, ECO:0000269|PubMed:19278996,
CC       ECO:0000269|PubMed:19380577, ECO:0000269|PubMed:21187438,
CC       ECO:0000269|PubMed:21525357}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBUNIT: Monomer in the absence of dsRNA. Homodimer in the presence of
CC       dsRNA. Interacts with DDX58/RIG-I (via CARD domain), MAVS/IPS1 and
CC       DDX60. Found in a complex with DDX58/RIG-I and IFIH1/MDA5. Interacts
CC       with ANKRD17. Directly interacts with ATG5 and ATG12, either as ATG5
CC       and ATG12 monomers or as ATG12-ATG5 conjugates (PubMed:17709747).
CC       {ECO:0000269|PubMed:17020950, ECO:0000269|PubMed:17190814,
CC       ECO:0000269|PubMed:17709747, ECO:0000269|PubMed:18411269,
CC       ECO:0000269|PubMed:19208642, ECO:0000269|PubMed:19278996,
CC       ECO:0000269|PubMed:21791617, ECO:0000269|PubMed:23711367}.
CC   -!- SUBUNIT: (Microbial infection) Interacts (via helicase C-terminal
CC       domain) with non-structural protein V of paramyxoviruses including
CC       human parainfluenza 2 virus, human parainfluenza 5 virus, measles
CC       virus, mumps virus, hendra virus and nipah virus.
CC       {ECO:0000269|PubMed:19403670}.
CC   -!- INTERACTION:
CC       Q9UKV8:AGO2; NbExp=2; IntAct=EBI-744193, EBI-528269;
CC       Q7L2E3:DHX30; NbExp=2; IntAct=EBI-744193, EBI-1211456;
CC       Q9UPY3:DICER1; NbExp=2; IntAct=EBI-744193, EBI-395506;
CC       P19525:EIF2AK2; NbExp=2; IntAct=EBI-744193, EBI-640775;
CC       P56537:EIF6; NbExp=2; IntAct=EBI-744193, EBI-372243;
CC       Q16666:IFI16; NbExp=2; IntAct=EBI-744193, EBI-2867186;
CC       O15226:NKRF; NbExp=2; IntAct=EBI-744193, EBI-766011;
CC       P11207:P/V (xeno); NbExp=2; IntAct=EBI-744193, EBI-6148694;
CC       P30927:P/V (xeno); NbExp=2; IntAct=EBI-744193, EBI-6599165;
CC       Q9EMA9:P/V (xeno); NbExp=2; IntAct=EBI-744193, EBI-6598728;
CC       Q9NUL3:STAU2; NbExp=2; IntAct=EBI-744193, EBI-722938;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19380577}.
CC   -!- INDUCTION: By interferon (IFN), virus infection, or intracellular
CC       dsRNA.
CC   -!- DOMAIN: The RLR CTR domain is capable of inhibiting dimerization and
CC       signaling of DDX58/RIG-I and also facilitates binding of dsRNA.
CC   -!- SIMILARITY: Belongs to the helicase family. RLR subfamily.
CC       {ECO:0000305}.
DR   EMBL; AK021416; BAB13818.1; -; mRNA.
DR   EMBL; BC014949; AAH14949.1; -; mRNA.
DR   CCDS; CCDS11416.1; -.
DR   RefSeq; NP_077024.2; NM_024119.2.
DR   RefSeq; XP_016880548.1; XM_017025059.1.
DR   RefSeq; XP_016880549.1; XM_017025060.1.
DR   PDB; 2RQA; NMR; -; A=546-678.
DR   PDB; 2W4R; X-ray; 2.60 A; A/B/C/D=537-678.
DR   PDB; 3EQT; X-ray; 2.00 A; A/B=541-678.
DR   PDBsum; 2RQA; -.
DR   PDBsum; 2W4R; -.
DR   PDBsum; 3EQT; -.
DR   SMR; Q96C10; -.
DR   BioGrid; 122553; 17.
DR   DIP; DIP-60792N; -.
DR   IntAct; Q96C10; 21.
DR   STRING; 9606.ENSP00000251642; -.
DR   iPTMnet; Q96C10; -.
DR   PhosphoSitePlus; Q96C10; -.
DR   BioMuta; DHX58; -.
DR   DMDM; 50401123; -.
DR   jPOST; Q96C10; -.
DR   MassIVE; Q96C10; -.
DR   MaxQB; Q96C10; -.
DR   PaxDb; Q96C10; -.
DR   PeptideAtlas; Q96C10; -.
DR   PRIDE; Q96C10; -.
DR   ProteomicsDB; 76141; -.
DR   TopDownProteomics; Q96C10; -.
DR   DNASU; 79132; -.
DR   Ensembl; ENST00000251642; ENSP00000251642; ENSG00000108771.
DR   GeneID; 79132; -.
DR   KEGG; hsa:79132; -.
DR   UCSC; uc002hyw.5; human.
DR   CTD; 79132; -.
DR   DisGeNET; 79132; -.
DR   EuPathDB; HostDB:ENSG00000108771.12; -.
DR   GeneCards; DHX58; -.
DR   HGNC; HGNC:29517; DHX58.
DR   HPA; HPA018670; -.
DR   HPA; HPA019570; -.
DR   MIM; 608588; gene.
DR   neXtProt; NX_Q96C10; -.
DR   OpenTargets; ENSG00000108771; -.
DR   PharmGKB; PA162383566; -.
DR   eggNOG; KOG0354; Eukaryota.
DR   eggNOG; COG1111; LUCA.
DR   GeneTree; ENSGT00940000153173; -.
DR   HOGENOM; HOG000230992; -.
DR   InParanoid; Q96C10; -.
DR   KO; K12649; -.
DR   OMA; HRAVGNY; -.
DR   OrthoDB; 1337630at2759; -.
DR   PhylomeDB; Q96C10; -.
DR   TreeFam; TF330258; -.
DR   Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR   ChiTaRS; DHX58; human.
DR   EvolutionaryTrace; Q96C10; -.
DR   GeneWiki; LGP2; -.
DR   GenomeRNAi; 79132; -.
DR   Pharos; Q96C10; Tbio.
DR   PRO; PR:Q96C10; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q96C10; protein.
DR   Bgee; ENSG00000108771; Expressed in 105 organ(s), highest expression level in left adrenal gland.
DR   ExpressionAtlas; Q96C10; baseline and differential.
DR   Genevisible; Q96C10; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0045824; P:negative regulation of innate immune response; IDA:UniProtKB.
DR   GO; GO:0039534; P:negative regulation of MDA-5 signaling pathway; IMP:UniProtKB.
DR   GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; IDA:UniProtKB.
DR   GO; GO:0032480; P:negative regulation of type I interferon production; IDA:UniProtKB.
DR   GO; GO:1900245; P:positive regulation of MDA-5 signaling pathway; ISS:UniProtKB.
DR   GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; ISS:UniProtKB.
DR   GO; GO:0032481; P:positive regulation of type I interferon production; ISS:UniProtKB.
DR   GO; GO:0045088; P:regulation of innate immune response; IDA:UniProtKB.
DR   GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR   GO; GO:0009615; P:response to virus; ISS:UniProtKB.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   Gene3D; 2.170.150.30; -; 1.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041204; RIG-I_C.
DR   InterPro; IPR038557; RLR_C_sf.
DR   InterPro; IPR021673; RLR_CTR.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   Pfam; PF18119; RIG-I_C; 1.
DR   Pfam; PF11648; RIG-I_C-RD; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51789; RLR_CTR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; ATP-binding; Coiled coil; Cytoplasm;
KW   Helicase; Host-virus interaction; Hydrolase; Immunity; Innate immunity;
KW   Metal-binding; Nucleotide-binding; Polymorphism; Reference proteome;
KW   RNA-binding; Zinc.
FT   CHAIN           1..678
FT                   /note="Probable ATP-dependent RNA helicase DHX58"
FT                   /id="PRO_0000102010"
FT   DOMAIN          11..188
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          350..514
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          539..669
FT                   /note="RLR CTR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01125"
FT   NP_BIND         24..31
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   REGION          572..655
FT                   /note="RNA-binding"
FT   COILED          489..546
FT                   /evidence="ECO:0000255"
FT   MOTIF           131..134
FT                   /note="DECH box"
FT   METAL           556
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01125"
FT   METAL           559
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01125"
FT   METAL           612
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01125"
FT   METAL           615
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01125"
FT   VARIANT         76
FT                   /note="T -> A (in dbSNP:rs34891485)"
FT                   /id="VAR_049336"
FT   VARIANT         95
FT                   /note="R -> Q (in dbSNP:rs35118457)"
FT                   /id="VAR_049337"
FT   VARIANT         425
FT                   /note="Q -> R (in dbSNP:rs2074158)"
FT                   /id="VAR_019394"
FT   VARIANT         523
FT                   /note="R -> Q (in dbSNP:rs2074160)"
FT                   /id="VAR_019395"
FT   MUTAGEN         634
FT                   /note="K->E: Abolishes RNA binding."
FT                   /evidence="ECO:0000269|PubMed:19208642,
FT                   ECO:0000269|PubMed:19278996"
FT   MUTAGEN         651
FT                   /note="K->E: Abolishes RNA binding."
FT                   /evidence="ECO:0000269|PubMed:19278996"
FT   CONFLICT        473
FT                   /note="R -> W (in Ref. 1; BAB13818)"
FT                   /evidence="ECO:0000305"
FT   HELIX           549..551
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   STRAND          553..556
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   TURN            557..559
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   STRAND          562..565
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   HELIX           566..568
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   STRAND          569..572
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   TURN            573..575
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   STRAND          576..579
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   HELIX           582..587
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   STRAND          588..590
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   STRAND          592..594
FT                   /evidence="ECO:0000244|PDB:2RQA"
FT   STRAND          597..599
FT                   /evidence="ECO:0000244|PDB:2RQA"
FT   STRAND          602..612
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   TURN            613..615
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   STRAND          618..625
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   STRAND          628..633
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   HELIX           635..637
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   STRAND          638..642
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   STRAND          645..647
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   HELIX           652..654
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   STRAND          655..657
FT                   /evidence="ECO:0000244|PDB:2W4R"
FT   HELIX           664..671
FT                   /evidence="ECO:0000244|PDB:3EQT"
FT   HELIX           675..677
FT                   /evidence="ECO:0000244|PDB:3EQT"
SQ   SEQUENCE   678 AA;  76613 MW;  859E1749C7313D06 CRC64;
     MELRSYQWEV IMPALEGKNI IIWLPTGAGK TRAAAYVAKR HLETVDGAKV VVLVNRVHLV
     TQHGEEFRRM LDGRWTVTTL SGDMGPRAGF GHLARCHDLL ICTAELLQMA LTSPEEEEHV
     ELTVFSLIVV DECHHTHKDT VYNVIMSQYL ELKLQRAQPL PQVLGLTASP GTGGASKLDG
     AINHVLQLCA NLDTWCIMSP QNCCPQLQEH SQQPCKQYNL CHRRSQDPFG DLLKKLMDQI
     HDHLEMPELS RKFGTQMYEQ QVVKLSEAAA LAGLQEQRVY ALHLRRYNDA LLIHDTVRAV
     DALAALQDFY HREHVTKTQI LCAERRLLAL FDDRKNELAH LATHGPENPK LEMLEKILQR
     QFSSSNSPRG IIFTRTRQSA HSLLLWLQQQ QGLQTVDIRA QLLIGAGNSS QSTHMTQRDQ
     QEVIQKFQDG TLNLLVATSV AEEGLDIPHC NVVVRYGLLT NEISMVQARG RARADQSVYA
     FVATEGSREL KRELINEALE TLMEQAVAAV QKMDQAEYQA KIRDLQQAAL TKRAAQAAQR
     ENQRQQFPVE HVQLLCINCM VAVGHGSDLR KVEGTHHVNV NPNFSNYYNV SRDPVVINKV
     FKDWKPGGVI SCRNCGEVWG LQMIYKSVKL PVLKVRSMLL ETPQGRIQAK KWSRVPFSVP
     DFDFLQHCAE NLSDLSLD
//
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