ID A0A2K5BX52_AOTNA Unreviewed; 1367 AA.
AC A0A2K5BX52;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:ENSANAP00000001003.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000001003.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000001003.1}
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 RefSeq; XP_012312726.1; XM_012457303.1.
DR STRING; 37293.ENSANAP00000001003; -.
DR Ensembl; ENSANAT00000009214.1; ENSANAP00000001003.1; ENSANAG00000005482.1.
DR GeneID; 105720662; -.
DR CTD; 54505; -.
DR GeneTree; ENSGT00940000157286; -.
DR OMA; SWFANMS; -.
DR OrthoDB; 1095660at2759; -.
DR Proteomes; UP000233020; Unplaced.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0043024; F:ribosomal small subunit binding; IEA:Ensembl.
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 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:UP000233020}.
FT DOMAIN 580..753
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 847..1024
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 281..308
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03068"
FT COMPBIAS 184..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1367 AA; 154996 MW; CE0B018BAE9C39C8 CRC64;
MGGKNKKHKV PAAAAVRAAV SASRAKSAEA GTAGEAQSKK PVSRPAPAVA ASSREPRVKQ
GPKIYSFNST NDSGGPANLD KSILKVVINN KLEQRIIGVI NEHKKQNNDK GIISGRLTAK
KLQDLYMALQ AFSFKTKDIE DAMTNTLLCG GDLHSALDWL CLNLSDDALP EGFSQEFEEQ
QPKSRPKFQS SQIQATISPP LQPKTKKHEE DPKIKPKKEE KNMDVNMKEW ILRYAEQQNE
EEKNENSKSL EEEEKFDPNE RYLHLAAKLL DAKEQAATFK LEKNKQGQKE AQEKIRKFQR
EMETLEDHPV FNPAIKISHQ QNERKKPPVA TEGESALNFN LFEKSAGATE EEKDKKKEPH
DIRNFDYTAR SWTGKSPKQF LIDWVRKNLP KSPNPSFEKV PVGRYWKCRV RVIKSEDDVL
VVCPTILTED GMQAQHLGAT LALYRLVKGQ SVHQLLPPTY RDVWLEWSDA EKKREELNKM
ETNKPRDLFI AKLLNKLKQQ QQQQQQHSEN KRENSEDPEE SWENLVSDED FSALSLESAN
VEDLEPVRNL FRKLQSTPKY QRLLKERQQL PIFKHRDSIV ETLKRHRVVV VAGETGSGKS
TQVPHFLLED LLLNEWGASK CNIVCTQPRR ISAVSLATRV CDELGCENGP GGRNSLCGYQ
IRMESRACES TRLLYCTTGV LLRKLQEDGL LSNVSHVIVD EVHERSVQSD FLLIILKEIL
QKRSDLHLIL MSATVDSEKF STYFTHCPIL RISGRSYPVE VFHLEDIIEE TGFVLEKDSE
YCQKFLEEEE EVTINVTSKA GGIKKYQEYI PVQTGANADL NPFYQKYSSR TQHAILYMNP
YKINLDLILE LLAYLDKSPQ FRNIEGAVLI FLPGLAHIQQ LYDLLSNDRR FYSERYRVIA
LHSILSTQDQ AAAFTLPPPG VRKIVLATNI AETGITIPDV VFVIDTGRTK ENKYHESSQM
SSLVETFVSK ASALQRQGRA GRVRDGFCFR MYTRERFEGF MDYSVPEILR VPLEELCLHI
MKCNLGSPED FLSKALDPPQ LQVISNAMNL LRRIGACELN EPKLTPLGQH LAALPVNVKI
GKMLIFGAIF GCLDPVATLA AVMTEKSPFT TPIGRKDEAD LAKSALAVAD SDHLTIYNAY
LGWKKARQEG GYRSEITYCR RNFLNRTSLL TLEDVKQELI KLVKAAGFSS STTSTSWEGN
RASQTLSFQE IALLKAVLVA GLYDNVGKII YTKSVDVTEK LACIVETAQG KAQVHPSSVN
RDLQTHGWLL YQEKIRYARV YLRETTLITP FPVLLFGGDI EVQHRERLLS IDGWIYFQAP
VKIAVIFKQL RVLIDSVLRK KLENPKMSLE NDKILQIITE LIKTENN
//
