DHX29_XENLA
ID DHX29_XENLA Reviewed; 1362 AA.
AC A3KMI0;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=ATP-dependent RNA helicase dhx29 {ECO:0000255|HAMAP-Rule:MF_03068};
DE EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_03068};
DE AltName: Full=DEAH box protein 29 {ECO:0000255|HAMAP-Rule:MF_03068};
GN Name=dhx29 {ECO:0000255|HAMAP-Rule:MF_03068};
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-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-binding RNA helicase involved in translation initiation.
CC Part of the 43S pre-initiation complex that is required for efficient
CC initiation on mRNAs of higher eukaryotes with structured 5'-UTRs by
CC promoting efficient NTPase-dependent 48S complex formation.
CC Specifically binds to the 40S ribosome near the mRNA entrance. Does not
CC possess a processive helicase activity. {ECO:0000255|HAMAP-
CC Rule:MF_03068}.
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:0000255|HAMAP-Rule:MF_03068};
CC -!- SUBUNIT: Part of the 43S pre-initiation complex (PIC).
CC {ECO:0000255|HAMAP-Rule:MF_03068}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03068}.
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DR EMBL; BC131891; AAI31892.1; -; mRNA.
DR RefSeq; NP_001091401.1; NM_001097932.1.
DR AlphaFoldDB; A3KMI0; -.
DR SMR; A3KMI0; -.
DR BioGRID; 674539; 1.
DR IntAct; A3KMI0; 1.
DR MaxQB; A3KMI0; -.
DR GeneID; 100049090; -.
DR KEGG; xla:100049090; -.
DR CTD; 100049090; -.
DR Xenbase; XB-GENE-995263; dhx29.L.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 100049090; Expressed in pancreas and 19 other tissues.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0043024; F:ribosomal small subunit binding; ISS:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0045948; P:positive regulation of translational initiation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_03068; DHX29; 1.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR034730; DHX29.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Helicase; Hydrolase;
KW Initiation factor; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..1362
FT /note="ATP-dependent RNA helicase dhx29"
FT /id="PRO_0000366029"
FT DOMAIN 576..749
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
FT DOMAIN 852..1021
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 89..109
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
FT COILED 285..305
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
FT MOTIF 696..699
FT /note="DEAH box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
FT COMPBIAS 42..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 589..596
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
SQ SEQUENCE 1362 AA; 153318 MW; 463432846A3DC380 CRC64;
MGGKNKKNRH GSSTAVQGAT AAANRPRAAA EPRPGGEDAA KKQTPRNSNV APGSKESNKQ
GPKTYSFASS SDSGVSVNHD KSVLKVVIEA KLEKRIISLI NEHKKLNSNK GTVSGRLTSK
KLQDLYMALQ KLSFKAEHIE EAMTNTVLYG GDLHAALDWL CLNLPDDALP EGFSQQFVEE
EQRARAKFQA PPQRPSAANE SATEKGEEGA SLKGNPELTM KEWILRYAEQ GSDDDDDDDD
VKEEEKETTL EKFDPNERYL ELTAKLLDAR AQATATKQDK DKQGQKEAQE RIRGYQQEMK
SLEDHPLFNP AVKIPEVKSE SKQPKPALPP SEDEPLNFNL FEKKENAPEE KAKKKPPLDI
RNFDYTSRSW TGKSPKQFLI DWCRKHYSKS PNPSFEKVPV GKYWKSRVKI IKSHDDVMCV
CPTIVTEDSM QAQHLAATLA LYELTKGQSV HQLLPPTYRN VWLEWSDAEK QVQEQNKTES
NKPRDQFITK LLNKLKVQQN QLKSCSQTQM MEDPEDSWEN LACDEEQHET CPSPLLPDDL
EPIRNIFRKS RDSMKYKRLL NDREQLPVFA RGNFILETLK RHRVIVVAGE TGSGKSTQVP
QFLLEDLLFN GGSPGKCNIV CTQPRRISAM SLATRVCEEL GCDSGPGGKN SLCGYQIRME
SRTGEATRLL YCTTGILLRK LQEDSMLKNI SHIIVDEVHE RTVQSDFLLI ILREILHKRS
DLHLVLMSAT VDCEKFSSYF THCPIIRISG RTFPVEVFHL EDVVEATGFV LEQDSEYCQK
FLEDEEEITL SVTGKGGSSK KYQEFIPAQS GTGLDLGARY QRYSSQTRHA VLYMNPNKIN
LDLILELLVF LDISPEYRNV EGAVLIFLPG LADIQQLYDI LSSDKRFHDR RRYKLIALHS
ILSSQDQAEA FILPPAGTRK IVLATNIAET GITIPDVVFV IDAGRTKENR YHESSQMSSL
VETFISKASA LQRQGRAGRV RNGYCFRLYT RERFESFMEY SVPEILRVPL EELCLHIMKC
DLGSPEDFLS KALDPPQLQV ISNAMSLLRK IGACELSQPK LTPLGQHLAA LPVNVKIGKM
LIFGAIFGCL DAVATLAATM TEKSPFVTPI GEKDRADLAK SSMAVANSDH VTIFRAYLGW
KAIRPEGYAA EMSYCRKNFL NRKALLTIED VKQELIRLVR AAGFECPRSV EANGLSSAMK
ALSAEETSLL KAILTAGLYD NVGKILFTKS VDITEKLACI VETAQGKAQV HPSSVNRDLQ
IYGWLLYQEK VKYSKVFLRE TTLISPFPVL LFGGDIAVQH RERLLTVDDW IHFQAPVKIA
VIFKELRILI ESVLKQKLEN PKMSLKDDMI LNIIKELIKT ER
