ID H2QQX0_PANTR Unreviewed; 1371 AA.
AC H2QQX0; A0A2J8JMQ3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 73.
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|EMBL:JAA02484.1, ECO:0000313|Ensembl:ENSPTRP00000028907.2,
GN ECO:0000313|VGNC:VGNC:6856};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000028907.2, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000028907.2, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:JAA02484.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA02484.1}, Skeletal muscle
RC {ECO:0000313|EMBL:JAA43900.1}, and Smooth vascular
RC {ECO:0000313|EMBL:JAA13757.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000028907.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; AACZ04069365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABC01008854; JAA02484.1; -; mRNA.
DR EMBL; GABF01008388; JAA13757.1; -; mRNA.
DR EMBL; GABE01000839; JAA43900.1; -; mRNA.
DR RefSeq; XP_001147019.1; XM_001147019.3.
DR STRING; 9598.ENSPTRP00000028907; -.
DR PaxDb; 9598-ENSPTRP00000028907; -.
DR Ensembl; ENSPTRT00000031298.3; ENSPTRP00000028907.2; ENSPTRG00000016875.3.
DR GeneID; 471819; -.
DR KEGG; ptr:471819; -.
DR CTD; 54505; -.
DR VGNC; VGNC:6856; DHX29.
DR eggNOG; KOG0920; Eukaryota.
DR GeneTree; ENSGT00940000157286; -.
DR HOGENOM; CLU_001832_1_4_1; -.
DR OMA; SWFANMS; -.
DR OrthoDB; 1095660at2759; -.
DR TreeFam; TF324744; -.
DR Proteomes; UP000002277; Chromosome 5.
DR Bgee; ENSPTRG00000016875; Expressed in fibroblast and 21 other cell types or tissues.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:Ensembl.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IBA:GO_Central.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:Ensembl.
DR GO; GO:0043024; F:ribosomal small subunit binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008494; F:translation activator activity; IEA:Ensembl.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IEA:Ensembl.
DR GO; GO:0045948; P:positive regulation of translational initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0042255; P:ribosome assembly; IEA:Ensembl.
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; 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; 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 2: Evidence at transcript level;
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:UP000002277}.
FT DOMAIN 584..757
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 851..1028
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 285..312
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03068"
FT COMPBIAS 188..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1371 AA; 155356 MW; B20C79E18342526D CRC64;
MGGKNKKHKA PAPAVVRAAV SASRAKSAEA GIAGEAQSKK PVSRPATAAA AAAAAGSREP
RVKQGPKIYS FNSTNDSSGP ANLDKSILKV VINNKLEQRI IGVINEHKKQ NSDKGMISGR
LTAKKLQDLY MALQAFSFKT KDIEDAMTNT LLYGGDLHSA LDWLCLNLSD DALPEGFSQE
FEEQQPKSRP KFQSPQIQAT ISPPLQPKTK TYEEDPKSKP KKEEKNMEVN MKEWILRYAE
QQNKEEKNEN SKSLEEEEKF DPNERYLHLA AKLLDAKEQA ATFKLEKNKQ GQKEAQEKIR
KFQREMETLE DHPVFNPAIK ISHQQNERKK PPVATEGEGA LNFNLFEKSA AATEEEKDKK
KEPHDVRNFD YTARSWTGKS PKQFLIDWVR KNLPKSPNPS FEKVPVGRYW KCRVRVIKSE
DDVLVVCPTI LTEDGMQAQH LGATLALYRL VKGQSVHQLL PPTYRDVWLE WSDAEKKREE
LNKMETNKPR DLFIAKLLNK LKQQQQQQQQ HSENKRENSE DPEESWENLV SDEDFSALSL
ESANVEDLEP VRNLFRKLQS TPKYQKLLKE RQQLPVFKHR DSIVETLKRH RVVVVAGETG
SGKSTQVPHF LLEDLLLNEW EASKCNIVCT QPRRISAVSL ANRVCDELGC ENGPGGRNSL
CGYQIRMESR ACESTRLLYC TTGVLLRKLQ EDGLLSNVSH VIVDEVHERS VQSDFLLIIL
KEILQKRSDL HLILMSATVD SEKFSTYFTH CPILRISGRS YPVEVFHLED IIEETGFVLE
KDSEYCQKFL EEEEEVTINV TSKAGGIKKY QEYIPVQTGA HADLNPFYQK YSSRTQHAIL
YMNPHKINLD LILELLAYLD KSPQFRNIEG AVLIFLPGLA HIQQLYDLLS NDRRFYSERY
KVIALHSILS TQDQAAAFTL PPPGVRKIVL ATNIAETGIT IPDVVFVIDT GRTKENKYHE
SSQMSSLVET FVSKASALQR QGRAGRVRDG FCFRMYTRER FEGFMDYSVP EILRVPLEEL
CLHIMKCNLG SPEDFLSKAL DPPQLQVISN AMNLLRKIGA CELNEPKLTP LGQHLAALPV
NVKIGKMLIF GAIFGCLDPV ATLAAVMTEK SPFTTPIGRK DEADLAKSAL AMADSDHLTI
YNAYLGWKKA RQEGGYRSEI TYCRRNFLNR TSLLTLEDVK QELIKLVKAA GFSSSTTSTS
WEGNRASQTL SFQEIALLKA VLVAGLYDNV GKIIYTKSVD VTEKLACIVE TAQGKAQVHP
SSVNRDLQTH GWLLYQEKIR YARVYLRETT LITPFPVLLF GGDIEVQHRE RLLSIDGWIY
FQAPVKIAVI FKQLRVLIDS VLRKKLENPK MSLENDRILQ IITELIKTEN N
//
