DHX15_DROME
ID DHX15_DROME Reviewed; 729 AA.
AC Q7K3M5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=ATP-dependent RNA helicase DHX15 homolog {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:O43143};
GN Name=Dhx15 {ECO:0000312|FlyBase:FBgn0033160};
GN ORFNames=CG11107 {ECO:0000312|FlyBase:FBgn0033160};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION.
RX PubMed=24782566; DOI=10.1126/scisignal.2004841;
RA Mosallanejad K., Sekine Y., Ishikura-Kinoshita S., Kumagai K., Nagano T.,
RA Matsuzawa A., Takeda K., Naguro I., Ichijo H.;
RT "The DEAH-box RNA helicase DHX15 activates NF-kappaB and MAPK signaling
RT downstream of MAVS during antiviral responses.";
RL Sci. Signal. 7:ra40-ra40(2014).
CC -!- FUNCTION: RNA helicase involved in mRNA processing and antiviral innate
CC immunity (By similarity). Acts as an activator of the p38 MAPK cascade
CC (PubMed:24782566). {ECO:0000250|UniProtKB:O43143,
CC ECO:0000269|PubMed:24782566}.
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 Evidence={ECO:0000250|UniProtKB:O43143};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX15/PRP43 sub-subfamily. {ECO:0000305}.
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DR EMBL; AE013599; AAF59269.1; -; Genomic_DNA.
DR EMBL; AE013599; AGB93299.1; -; Genomic_DNA.
DR EMBL; AY058484; AAL13713.1; -; mRNA.
DR RefSeq; NP_001260766.1; NM_001273837.1.
DR RefSeq; NP_610269.1; NM_136425.3.
DR AlphaFoldDB; Q7K3M5; -.
DR SMR; Q7K3M5; -.
DR IntAct; Q7K3M5; 5.
DR STRING; 7227.FBpp0088040; -.
DR PaxDb; Q7K3M5; -.
DR PRIDE; Q7K3M5; -.
DR DNASU; 35654; -.
DR EnsemblMetazoa; FBtr0088966; FBpp0088040; FBgn0033160.
DR EnsemblMetazoa; FBtr0336909; FBpp0307849; FBgn0033160.
DR GeneID; 35654; -.
DR KEGG; dme:Dmel_CG11107; -.
DR UCSC; CG11107-RA; d. melanogaster.
DR CTD; 1665; -.
DR FlyBase; FBgn0033160; Dhx15.
DR VEuPathDB; VectorBase:FBgn0033160; -.
DR eggNOG; KOG0925; Eukaryota.
DR GeneTree; ENSGT00940000155800; -.
DR HOGENOM; CLU_001832_5_11_1; -.
DR InParanoid; Q7K3M5; -.
DR OMA; DHDLKRY; -.
DR OrthoDB; 354219at2759; -.
DR PhylomeDB; Q7K3M5; -.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 35654; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 35654; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033160; Expressed in wing disc and 25 other tissues.
DR ExpressionAtlas; Q7K3M5; baseline and differential.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0005681; C:spliceosomal complex; ISS:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; ISS:FlyBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:FlyBase.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IGI:FlyBase.
DR CDD; cd17973; DEXHc_DHX15; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044756; DHX15_DEXHc.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 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.
PE 2: Evidence at transcript level;
KW ATP-binding; Helicase; Hydrolase; Immunity; Innate immunity;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Reference proteome;
KW RNA-binding.
FT CHAIN 1..729
FT /note="ATP-dependent RNA helicase DHX15 homolog"
FT /id="PRO_0000455079"
FT DOMAIN 82..246
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 271..451
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 193..196
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 95..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 729 AA; 82652 MW; 5C14D4338E6403A8 CRC64;
MSKRRIEVGE TYGSKAKKDP EASSSSAAAA AGTVAQILGG FVPNKQPPTM NPLTNTPYSQ
RYQNLYKKRI ALPVFEYQAD FMRLLSLHQC IVLVGETGSG KTTQIPQWCV DFAVSKGRKG
VSCTQPRRVA AMSVAQRVSE EMDVKLGEEV GYSIRFEDCS TAKTLLKYMT DGMLLREAMS
DPMLDQYQVI LLDEAHERTL ATDILMGVLK EVIRQRSDLK LVVMSATLDA GKFQQYFDNA
PLMKVPGRTH PVEIFYTPEP ERDYLEAAIR TVIQIHMCEE IEGDILMFLT GQEEIEEACK
RIKREIDNLG SEIGELKCIP LYSTLPPNLQ QRIFEPAPPP NANGAIGRKV VVSTNIAETS
LTIDGVVFVI DPGFAKQKVY NPRIRVESLL VSPISKASAQ QRSGRAGRTR PGKCFRLYTE
KAFKNEMQDN TYPEILRSNL GTVVLQLKKL GIDDLVHFDF MDPPAPETLM RALELLNYLA
ALDDDGNLTD LGAVMSEFPL DPQLAKMLIA SCQHNCSNEI LSITAMLSVP QCFVRPNEAK
KAADEAKMRF AHIDGDHLTL LNVYHAFKQS SEDPNWCYEN FINFRSLKSA DNVRQQLARI
MDRFNLRRTS TEFTSKDYYV NIRKALVQGF FMQVAHLERT GYYLTIKDNQ NVQLHPSTCL
DHKPDWVIYN EFVLTTKNYI RTVTDVKPEW LCCLAPQYYD LNNFPQCEAK RQLELLQQRL
ETKQYQKGF
