DX39B_CAEEL
ID DX39B_CAEEL Reviewed; 425 AA.
AC Q18212; Q17323;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Spliceosome RNA helicase DDX39B homolog;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein UAP56;
GN Name=hel-1 {ECO:0000312|WormBase:C26D10.2a};
GN ORFNames=C26D10.2 {ECO:0000312|WormBase:C26D10.2a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-425.
RA Melnick M.B., Lorenz L.J., Eberl D., Perrimon N.;
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH RSR-1.
RX PubMed=12944400; DOI=10.1074/jbc.m306856200;
RA McCracken S., Longman D., Johnstone I.L., Caceres J.F., Blencowe B.J.;
RT "An evolutionarily conserved role for SRm160 in 3'-end processing that
RT functions independently of exon junction complex formation.";
RL J. Biol. Chem. 278:44153-44160(2003).
RN [4]
RP FUNCTION.
RX PubMed=12810918; DOI=10.1261/rna.5480803;
RA MacMorris M., Brocker C., Blumenthal T.;
RT "UAP56 levels affect viability and mRNA export in Caenorhabditis elegans.";
RL RNA 9:847-857(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23149939; DOI=10.1128/mcb.01298-12;
RA Shiimori M., Inoue K., Sakamoto H.;
RT "A specific set of exon junction complex subunits is required for the
RT nuclear retention of unspliced RNAs in Caenorhabditis elegans.";
RL Mol. Cell. Biol. 33:444-456(2013).
CC -!- FUNCTION: Required for spliced RNA export out of the nucleus
CC (PubMed:23149939). May play a role in spliceosome assembly.
CC {ECO:0000269|PubMed:12810918, ECO:0000269|PubMed:23149939}.
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: Interacts with rsr-1/SRm160. {ECO:0000269|PubMed:12944400}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown prevents germ cells from
CC entering meiosis and results in the accumulation of unspliced mRNAs in
CC the cytoplasm. {ECO:0000269|PubMed:23149939}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DECD subfamily.
CC {ECO:0000305}.
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DR EMBL; BX284602; CAA91120.1; -; Genomic_DNA.
DR EMBL; U08102; AAB65852.1; -; mRNA.
DR PIR; T19484; T19484.
DR RefSeq; NP_001021985.1; NM_001026814.3.
DR AlphaFoldDB; Q18212; -.
DR SMR; Q18212; -.
DR BioGRID; 39662; 29.
DR IntAct; Q18212; 8.
DR STRING; 6239.C26D10.2a; -.
DR iPTMnet; Q18212; -.
DR EPD; Q18212; -.
DR PaxDb; Q18212; -.
DR PeptideAtlas; Q18212; -.
DR EnsemblMetazoa; C26D10.2a.1; C26D10.2a.1; WBGene00001840.
DR GeneID; 174333; -.
DR KEGG; cel:CELE_C26D10.2; -.
DR UCSC; C26D10.2a; c. elegans.
DR CTD; 174333; -.
DR WormBase; C26D10.2a; CE03025; WBGene00001840; hel-1.
DR eggNOG; KOG0329; Eukaryota.
DR GeneTree; ENSGT00940000154912; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q18212; -.
DR OMA; INFELPM; -.
DR OrthoDB; 779000at2759; -.
DR PhylomeDB; Q18212; -.
DR BRENDA; 3.6.4.13; 1045.
DR Reactome; R-CEL-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-CEL-72187; mRNA 3'-end processing.
DR Reactome; R-CEL-73856; RNA Polymerase II Transcription Termination.
DR PRO; PR:Q18212; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001840; Expressed in embryo and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0005667; C:transcription regulator complex; IPI:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0008134; F:transcription factor binding; IPI:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IGI:WormBase.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:WormBase.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 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; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding; Spliceosome.
FT CHAIN 1..425
FT /note="Spliceosome RNA helicase DDX39B homolog"
FT /id="PRO_0000055079"
FT DOMAIN 72..245
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 257..418
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 41..69
FT /note="Q motif"
FT MOTIF 192..195
FT /note="DECD box"
FT COMPBIAS 1..17
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 211..217
FT /note="Missing (in Ref. 2; AAB65852)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 425 AA; 48493 MW; 7D6041E38AC3A44F CRC64;
MEEEQLLDYE EEQEEIQDKQ PEVGGGDARK TKGTYASIHS SGFRDFLLKP EILRAIGDCG
FEHPSEVQHE CIPQAILGMD VVCQAKSGMG KTAVFVITTL QQLEPVDGEV SVVCMCHTRE
LAFQISKEYE RFSKYLPGVK VAVFFGGMAI KKDEERLAND CPHIVVGTPG RMLALARSGK
LKLDKVKYFV LDECDKMIGD ADMRRDVQEI VKMTPQQKQV MMFSATLPKE LRTVCKRFMQ
DPMEVYVDDE AKLTLHGLQQ HYVKLKEAEK NRRLLNLLDA LEFNQVVIFV KAVKRCEALH
QLLTEQNFPS IAIHRQMAQE ERLSRYQAFK DFQKRILVAT DLFGRGMDIE RVNIVFNYDM
PEDSDSYLHR VARAGRFGTK GLAITFVSDE NDAKTLNSVQ DRFDISITEL PEKIDVSTYI
EGRTN
