DDX42_XENLA
ID DDX42_XENLA Reviewed; 947 AA.
AC Q7ZY47;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=ATP-dependent RNA helicase DDX42;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q86XP3};
DE AltName: Full=DEAD box protein 42;
GN Name=ddx42;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent RNA helicase. Binds to partially double-
CC stranded RNAs (dsRNAs) in order to unwind RNA secondary structures.
CC Unwinding is promoted in the presence of single-strand binding
CC proteins. Mediates also RNA duplex formation thereby displacing the
CC single-strand RNA binding protein. ATP and ADP modulate its activity:
CC ATP binding and hydrolysis by DDX42 triggers RNA strand separation,
CC whereas the ADP-bound form of the protein triggers annealing of
CC complementary RNA strands. {ECO:0000250|UniProtKB:Q86XP3}.
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:Q86XP3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86XP3}. Nucleus
CC {ECO:0000250|UniProtKB:Q86XP3}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX42 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC043977; AAH43977.1; -; mRNA.
DR RefSeq; NP_001080569.1; NM_001087100.1.
DR AlphaFoldDB; Q7ZY47; -.
DR SMR; Q7ZY47; -.
DR BioGRID; 98503; 1.
DR IntAct; Q7ZY47; 1.
DR DNASU; 380261; -.
DR GeneID; 380261; -.
DR KEGG; xla:380261; -.
DR CTD; 380261; -.
DR Xenbase; XB-GENE-972673; ddx42.L.
DR OrthoDB; 245118at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 380261; Expressed in brain and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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; IPR000629; RNA-helicase_DEAD-box_CS.
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; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..947
FT /note="ATP-dependent RNA helicase DDX42"
FT /id="PRO_0000280062"
FT DOMAIN 281..456
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 484..629
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 112..152
FT /evidence="ECO:0000255"
FT MOTIF 250..278
FT /note="Q motif"
FT MOTIF 404..407
FT /note="DEAD box"
FT COMPBIAS 34..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 294..301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 947 AA; 104079 MW; F3ACC9B7400642C9 CRC64;
MNWNKGGSGN KRGFGFGGFA ISTGKKEEPK LPQVSHSAFQ SASSKYGSTS NQLPSFYKIG
SKRANFDEEN SYFDDEEEDS SNVDLPYIPA ENSPTRQQLR SKTDSDSEED PLEAFMAEVE
DQAAKDMRKL EERDKEKANA RGIRDDIEEE DDQEAYFRYM AENPTAGLVP EEEEDNLEYD
SDGNPIAPTT KRIIDPLPPI DHTEIEYPPF EKNFYEEHEA ITSQTPQQIT ELRHKLNLRV
SGAAPPRLCS SFAHFGFDEQ LLHQIRKSEY TQPTPIQCQG IPVALSGRDM IGIAKTGSGK
TAAFIWPILV HIMDQKELQP ADGPIAVIVC PTRELCQQIH SECKRFGKAY NLRSVAVYGG
GSMWEQAKAL QEGAEIVVCT PGRLIDHVKK KATNLQRVTY LVFDEADRMF DMGFEYQVRS
IANHVRPDRQ TLLFSATFRK KIEKLARDIL VDPIRVVQGD IGEANEDITQ VVEILPSGPE
KWTWLTRRLV EFTSTGSVLV FVTKKANAEE LAANLRQDDH PLGLLHGDMD QSERNKVISD
FKKKSIPVLV ATDVAARGLD IPSIKTVVNY DVARDIDTHT HRIGRTGRAG EKGVAYTLLT
SKESNFAGDL VRNLEGANQY VSKELLDLAM QNSWFRKSRF KAGKGKKLNI GGGGLGYRER
PGLGAESSEH GTGGNVMSNY EAFKPSGGAM GDRLSAMKSA FQSQYKNHFV AASASTQKTG
TSSINSGAWT SAGSLSSVPS AHPPSGKLPA EAAPPPVHTA MLGFTSSGTL SSIPTGYPAN
ISSASYPAAT LFGARDGASA GTESGGRERH SDSKGRHGDS HRPSDREGYR HGDGHRHSSS
SRHGERNGGE GRRESSRDGR RDSSRDGESR RDGSRDGGEG RRESSRDGEG RRESSRDGDG
RRESSGDGRR EVVGDDGDSR KEGTREAKTD TFAIPVPPKR KKSRWDS
