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ATP-dependent RNA helicase WM6 (DEAD box protein UAP56) (Dmrnahel) (EC 3.6.4.13) (HEL/UAP56)

 DX39B_DROME             Reviewed;         424 AA.
Q27268; Q540X0; Q9VMQ1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 154.
RecName: Full=ATP-dependent RNA helicase WM6;
Short=DEAD box protein UAP56;
Short=Dmrnahel;
EC=3.6.4.13;
AltName: Full=HEL/UAP56;
Name=Hel25E; Synonyms=Dbp25F, hel, WM6; ORFNames=CG7269;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Oregon-R; TISSUE=Embryo;
PubMed=7808417; DOI=10.1007/BF00282229;
Warbrick E., Glover D.;
"A Drosophila gene encoding a DEAD box RNA helicase can suppress loss
of wee1/mik1 function in Schizosaccharomyces pombe.";
Mol. Gen. Genet. 245:654-657(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
PubMed=9215899;
Eberl D.F., Lorenz L.J., Melnick M.B., Sood V., Lasko P., Perrimon N.;
"A new enhancer of position-effect variegation in Drosophila
melanogaster encodes a putative RNA helicase that binds chromosomes
and is regulated by the cell cycle.";
Genetics 146:951-963(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE EXON JUNCTION
COMPLEX.
PubMed=11696332; DOI=10.1016/S0960-9822(01)00532-2;
Gatfield D., Le Hir H., Schmitt C., Braun I.C., Koecher T., Wilm M.,
Izaurralde E.;
"The DExH/D box protein HEL/UAP56 is essential for mRNA nuclear export
in Drosophila.";
Curr. Biol. 11:1716-1721(2001).
[7]
FUNCTION.
PubMed=12743041; DOI=10.1093/emboj/cdg233;
Herold A., Teixeira L., Izaurralde E.;
"Genome-wide analysis of nuclear mRNA export pathways in Drosophila.";
EMBO J. 22:2472-2483(2003).
-!- FUNCTION: Required for mRNA export out of the nucleus. Probable
RNA helicase that may regulate entry into mitosis by down-
regulating the expression of other genes whose activity may be
rate-limiting for entry into mitosis during embryogenesis. Binds
to salivary gland chromosomes and modifies position effect
variegation. Promotes an open chromatin structure that favors
transcription during development by regulating the spread of
heterochromatin. {ECO:0000269|PubMed:11696332,
ECO:0000269|PubMed:12743041, ECO:0000269|PubMed:9215899}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Component of the spliceosome (Probable). Interacts with
the exon junction complex. {ECO:0000269|PubMed:11696332,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleus speckle
{ECO:0000269|PubMed:11696332, ECO:0000269|PubMed:9215899}.
Note=Locates to nuclei of embryos and ovaries, but disappears in
mitotic domains of embryos as chromosomes condense.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
{ECO:0000269|PubMed:9215899}.
-!- SIMILARITY: Belongs to the DEAD box helicase family. DECD
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; X79802; CAA56197.1; -; mRNA.
EMBL; L06018; AAB65835.1; -; Genomic_DNA.
EMBL; AE014134; AAF52261.1; -; Genomic_DNA.
EMBL; AE014134; AAN10544.1; -; Genomic_DNA.
EMBL; AE014134; AAN10545.1; -; Genomic_DNA.
EMBL; AY118921; AAM50781.1; -; mRNA.
PIR; S51601; S51601.
RefSeq; NP_723089.1; NM_164646.3.
RefSeq; NP_723090.1; NM_164647.1.
RefSeq; NP_723091.1; NM_164648.2.
UniGene; Dm.3332; -.
ProteinModelPortal; Q27268; -.
SMR; Q27268; -.
BioGrid; 59949; 48.
DIP; DIP-20199N; -.
IntAct; Q27268; 9.
STRING; 7227.FBpp0078754; -.
PaxDb; Q27268; -.
PRIDE; Q27268; -.
EnsemblMetazoa; FBtr0079123; FBpp0078754; FBgn0014189.
EnsemblMetazoa; FBtr0079124; FBpp0078755; FBgn0014189.
EnsemblMetazoa; FBtr0079125; FBpp0078756; FBgn0014189.
GeneID; 33781; -.
KEGG; dme:Dmel_CG7269; -.
CTD; 33781; -.
FlyBase; FBgn0014189; Hel25E.
eggNOG; KOG0329; Eukaryota.
eggNOG; COG0513; LUCA.
GeneTree; ENSGT00830000128348; -.
InParanoid; Q27268; -.
KO; K12812; -.
OMA; CRKFMQN; -.
OrthoDB; EOG091G0H5W; -.
PhylomeDB; Q27268; -.
Reactome; R-DME-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-DME-72187; mRNA 3'-end processing.
GenomeRNAi; 33781; -.
PRO; PR:Q27268; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0014189; -.
ExpressionAtlas; Q27268; baseline and differential.
Genevisible; Q27268; DM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0005681; C:spliceosomal complex; ISS:FlyBase.
GO; GO:0000346; C:transcription export complex; ISS:FlyBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004004; F:ATP-dependent RNA helicase activity; ISS:FlyBase.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
GO; GO:0006338; P:chromatin remodeling; IMP:FlyBase.
GO; GO:0006406; P:mRNA export from nucleus; IMP:FlyBase.
GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:FlyBase.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:FlyBase.
GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central.
CDD; cd00079; HELICc; 1.
InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
Pfam; PF00270; DEAD; 1.
Pfam; PF00271; Helicase_C; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51195; Q_MOTIF; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Helicase; Hydrolase; mRNA processing;
mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome;
RNA-binding; Spliceosome.
CHAIN 1 424 ATP-dependent RNA helicase WM6.
/FTId=PRO_0000055080.
DOMAIN 72 246 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 258 419 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 85 92 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 41 69 Q motif.
MOTIF 193 196 DECD box.
SEQUENCE 424 AA; 48652 MW; CE132476090E1AFE CRC64;
MADNDDLLDY EDEEQTETTA VENQEAPKKD VKGTYVSIHS SGFRDFLLKP EILRAIVDCG
FEHPSEVQHE CIPQAVLGMD ILCQAKSGMG KTAVFVLATL QQLEPSDNNT CHVLVMCHTR
ELAFQISKEY ERFSKYMPTV KVAVFFGGMA IQKDEETLKS GTPHIVVGTP GRILALIRNK
KLNLKLLKHF VLDECDKMLE QLDMRRDVQE IFRSTPHGKQ VMMFSATLSK DIRPVCKKFM
QDPMEVYVDD EAKLTLHGLQ QHYVNLKENE KNKKLFELLD VLEFNQVVIF VKSVQRCVAL
SQLLTEQNFP AIGIHRGMTQ EERLNRYQQF KDFQKRILVA TNLFGRGMDI ERVNIVFNYD
MPEDSDTYLH RVARAGRFGT KGLAITFVSD ENDAKILNEV QDRFDVNISE LPEEIDLSTY
IEGR


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