ID G3PV10_GASAC Unreviewed; 1376 AA.
AC G3PV10;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:ENSGACP00000021447.1};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000021447.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000021447.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000021447.1}
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|HAMAP-Rule:MF_03068};
CC -!- SUBUNIT: Part of the 43S pre-initiation complex (PIC).
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 STRING; 69293.ENSGACP00000021447; -.
DR Ensembl; ENSGACT00000021488.1; ENSGACP00000021447.1; ENSGACG00000016244.1.
DR eggNOG; KOG0920; Eukaryota.
DR GeneTree; ENSGT00940000157286; -.
DR InParanoid; G3PV10; -.
DR OMA; SWFANMS; -.
DR TreeFam; TF324744; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000016244; Expressed in head kidney and 10 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; 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; 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; 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; 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}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03068};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_03068};
KW Hydrolase {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:UP000007635}.
FT DOMAIN 595..768
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 862..1040
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 21..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1376 AA; 154701 MW; 6B5B94028F71C871 CRC64;
MGGKKKKSAV QAAAAAMAAA AAAGRTGAAP AEEPKKQPAN NNKPAKPEWH NSVFPRVFPA
PKTYSLANTS QVDTGGVTDK SILKVAIQAE LEKKIIKLIN DFREENGDKG PISGRLTNKK
LLDLYTALQK FNFKREHIEE AMKSSVLYGG DLHSALDWLC LNLRDEELPE GFTQQMQEES
QRSRPRFQPL VQEKPAPPSP KAPSEHRREP AKVTEKDDAA SMKDWILRYA EQSSDEEEEE
EVGKKTHNPE LEEKFDPNDR YLALTAQLYD AKEMAATTKA KGDKAGQRMA QDRIRIIQQE
MKPLESHPVF NPAIKVVDVP QKEKKTLPVS ENKGDANFNL FEQTEKPPPA AKVPKKNEPK
DIRNFDYTAR SWTGKSPKQF LIDWVRKNLP KSPAPAFHKV AAGRYWRSKV RVQRTEDVLE
VCPTILTEDS MQAQHLAATL ALYTLVKGQS VHQLLPPTYR DVWLEWRDSE QHQQEESRTA
ANKPRDQFIS RLLTRLKQQQ QNQHPSVPEV GSQGQRGQGS AGDEEPEESW ENLAGLDIVE
GGEELEDRSE KRARAEGALE ASRELLMKLK KSPLAHKLKA QREQLPVFQH RHRVLEALQR
HPVVVVAGET GSGKSTQIPQ FLLEEMLTGG KVAKPCNIVV TQPRRISAMS LACRVSQEMG
CEDGPGSKSS LCGYQIRMEN ESGEWTRLLY CTTGVLLRKL QHDRHLSSLT HIIVDEVHER
SVQSDFLLTI LKDVVMRRSD LQLILMSATV DCCKFSNYFN RCPVINIPGR TFPVEVFHLE
DIVEQTGYVL EKDSEYSQKI LEDEEEVSIS ISQKGGRTAQ HQEVILRDPS SGWDLGPDLD
HFSSRTRQVL QYMNPNKINM DLLVDLIDYL DKSPQFARLD GAVLVFLPGL AHIQQLHDLL
TSDKRFRDKN RYRIVALHST LSSKDQAAAF TVPPAGSRKI VLSTNIAETG VTIPDVVFVI
DTGKTKENKY HESSQMSSLV ETFVSKASAL QRQGRAGRVQ NGFCFRLYPK FRFDAFMEYS
IPEILRVPLE ELCLHIMKCQ YGSPEEFLSR ALDAPQPQSV SNAVNLLRKI GACRPDNHLL
TPLGHHLAGL PVNVKIGKML IYGAILGCLE PIATIAAAIS EKSPFSTPMN RKEEANLAKA
ALALANSDHL TIYNAYLGWK NSQTDGQRAE MCFCRQHFLN RTALVTIESV KHELMRMMEQ
AGFWSSRSKP QAAAAALSKH QISVLNAVLT AGLYDSVARV LCTPSVDVLE RVVCTVETPQ
GKAQVHPSSV NRNLQTHGWL LYQEKVKYGK IYLRDTSLIS PFPVLLFGGD IDIQHRERLI
SVDGWILFQA PVRIGVIFKH LRKLMDSLLE RKLENPRMSL EGEKTIHMIL DLIKSE
//
