ID A0A452EHZ7_CAPHI Unreviewed; 1353 AA.
AC A0A452EHZ7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=ATP-dependent RNA helicase DHX29 {ECO:0000256|HAMAP-Rule:MF_03068};
DE EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_03068};
DE AltName: Full=DEAH box protein 29 {ECO:0000256|HAMAP-Rule:MF_03068};
GN Name=DHX29 {ECO:0000256|HAMAP-Rule:MF_03068,
GN ECO:0000313|Ensembl:ENSCHIP00000011526.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000011526.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000011526.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000011526.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|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:0000256|ARBA:ARBA00001556, ECO:0000256|HAMAP-
CC Rule:MF_03068};
CC -!- SUBUNIT: Part of the 43S pre-initiation complex (PIC) that contains at
CC least Met-tRNA, EIF1, EIF1A (EIF1AX or EIF1AY), EIF2S1, EIF2S2, EIF2S3,
CC EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J,
CC EIF3K, EIF3L, EIF3M, DHX29 and the 40S ribosomal subunit.
CC {ECO:0000256|HAMAP-Rule:MF_03068}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03068}.
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DR EMBL; LWLT01000017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSCHIT00000019316.1; ENSCHIP00000011526.1; ENSCHIG00000013568.1.
DR GeneTree; ENSGT00940000157286; -.
DR Proteomes; UP000291000; Chromosome 20.
DR Bgee; ENSCHIG00000013568; Expressed in longissimus thoracis muscle and 16 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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 CDD; cd17975; DEXHc_DHX29; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF145; ATP-DEPENDENT RNA HELICASE DHX29; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03068}; Coiled coil {ECO:0000256|HAMAP-Rule:MF_03068};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03068};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_03068};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03068};
KW Initiation factor {ECO:0000256|HAMAP-Rule:MF_03068};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03068}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03068};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000}.
FT DOMAIN 577..750
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 844..1012
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 278..305
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03068"
FT COMPBIAS 184..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1353 AA; 153693 MW; C898086CFC989F2A CRC64;
MGGKNKKHKT PGAAAVRAAV SASRAKSAEA GATGEAQNKP VSRPAPAAAA SAREPRVKQG
PKIYSFNSAN DSGGPANLDK SILKVVINNK LEQKIIGVIN EHKKQNNDKG VISGRLTAKK
LQDLYMALQA FSFKTKDIED AMTNTLLHGG DLHSALDWLC LNLSDDALPE GFSQEFEEQQ
PKSRPKFQYP QTQATISPPL QPKTRKQEED PKIMPKKDGK NLEVNMKEWI LRYAEQQNEE
KSETSKSLEE EKFDPNERYL HLAAKLLDAK EQAATFKLEK NKQGQKETQE KIRKFQREME
TLEDHPVFNP AIKISHQQNE RKKPPVVTEG ESALNFNLFE KSTAAPEEER EKKKEPHDVR
NFDYTARSWT GKSPKQFLID WVRKNLPKSP NPSFEKVAVG RYWKCRVRVI KSEDDVLVVC
PTILTEDGMQ AQHLGATLAL YRLVKGQSVH QLLPPTYRDV WLEWSDAEKK KEELNKMETN
KPRDLFIAKL LNKLKQQQQQ QQQHSENKRE NSEDPEESWE NLVSDEDFSA LSLESEKVED
LEPVRNLFRK LQSTPKYQRL LKERQQLPVF KHRSSIVETL KRHRVVVVAG ETGSGKSTQV
PHFLLEDLLL NEWGATKCNI VCTQPRRISA VSLATRVCDE LGCENGPGGK NSLCGYQIRM
ESRASESTRL LYCTTGVLLR KLQEDGLLTN VSHVIVDEVH ERSVQSDFLL IILKEILQKR
SDLHLILMSA TVDSEKFSTY FTHCPILRIS GRSYPVEVFH LEDIIEETGF VLEKDSEYCQ
KFLEEEEEIT INVTTKAGGI KKYQEYIPVQ TGTSADLNPF YQKYSSRTQH AILYMNPHKI
NLDLVLELLI YLDRSPQFKN VEGAVLIFLP GLAHIQQLYD LLSTDRRFFS ERYKVIALHS
ILSTQDQAAA FTLPPQGVRK VKLSTSNLYV IHLRTVHEND YHQRHSQMSS LVETFVSKAS
ALQRQGRAGR VRDGFCFRMY TRERFEGFMD YSVPEILRVP LEELCLHIMK CNLGSPEDFL
SKALDPPQLQ VISNAMNLLR KIGACELNEP KLTPLGQHLA ALPVNVKIGK MLIFGAIFGC
LDPVATLAAV MTEKSPFTTP IGRKDEADLA KSALAMADSD HLTIYNAYLG WKKARQEGGY
RSEIAYCRKN FLNRTSLLTL EDVKQELIKL VKAAGFLSST TSNSFEGNRA TQTLSFQEIA
LLKAVLTAGL YDNVGKIMYT KSVDITEKLA CIVETAQGKA QVHPSSVNRD LQIYGWLLYQ
EKIRYARVYL RETTLITPFP VLLFGGDIEV QHRERLISVD GWIYFQAPVK IAVIFKQLRV
LIDSVLRKKL ENPKMSLEND KILQIITELI KTE
//
