ID G0PH28_CAEBE Unreviewed; 452 AA.
AC G0PH28;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit G {ECO:0000256|HAMAP-Rule:MF_03006};
DE Short=eIF3g {ECO:0000256|HAMAP-Rule:MF_03006};
DE AltName: Full=Eukaryotic translation initiation factor 3 RNA-binding subunit {ECO:0000256|HAMAP-Rule:MF_03006};
DE Short=eIF-3 RNA-binding subunit {ECO:0000256|HAMAP-Rule:MF_03006};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 4 {ECO:0000256|HAMAP-Rule:MF_03006};
GN Name=eif-3.G {ECO:0000256|HAMAP-Rule:MF_03006};
GN ORFNames=CAEBREN_07157 {ECO:0000313|EMBL:EGT56048.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is involved in protein
CC synthesis of a specialized repertoire of mRNAs and, together with other
CC initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation. This
CC subunit can bind 18S rRNA. {ECO:0000256|HAMAP-Rule:MF_03006}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03006}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit G family. {ECO:0000256|HAMAP-
CC Rule:MF_03006}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000256|ARBA:ARBA00010290}.
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DR EMBL; GL380459; EGT56048.1; -; Genomic_DNA.
DR AlphaFoldDB; G0PH28; -.
DR STRING; 135651.G0PH28; -.
DR EnsemblMetazoa; CBN07157.1; CBN07157.1; WBGene00145882.
DR eggNOG; KOG0073; Eukaryota.
DR eggNOG; KOG0122; Eukaryota.
DR HOGENOM; CLU_043595_0_0_1; -.
DR InParanoid; G0PH28; -.
DR OMA; TNLPQDM; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR CDD; cd04154; Arl2; 1.
DR CDD; cd12933; eIF3G; 1.
DR CDD; cd12408; RRM_eIF3G_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_03006; eIF3g; 1.
DR InterPro; IPR045873; Arl2.
DR InterPro; IPR044612; ARL2/3.
DR InterPro; IPR017334; eIF3_g.
DR InterPro; IPR024675; eIF3g_N.
DR InterPro; IPR034240; eIF3G_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR45697:SF2; ADP-RIBOSYLATION FACTOR-LIKE PROTEIN 2; 1.
DR PANTHER; PTHR45697; ADP-RIBOSYLATION FACTOR-LIKE PROTEIN 2-RELATED; 1.
DR Pfam; PF00025; Arf; 1.
DR Pfam; PF12353; eIF3g; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS51417; ARF; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03006};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_03006}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03006}; Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 199..282
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 169..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 51171 MW; 22AB54A02C54F158 CRC64;
MAGINSITTA PEVVSWAEAV EQDNSPHVQE GADGIRTETA FTEVDGVRYK VGIAEKLAAN
SNFPNFQVVT QFKVINKRVP KVVADRKKWV KFGACKGEPA GPQVATTYVA EEVEMQFTRN
RAGEQILDVQ EDKQTAKATS REHCRHCKGN DHWSTHCPYK VMYQLDEEND ANNDPQQDRN
AMGLRGDGRQ IDRNRSDENT CRVTNLPQEM NEDELRDVFG KIGRVIRIFI ARDKITALPK
GFAFVTFESR DDAARAIAEL NDIRMYHMMG FLKILRKQRA REREMRILIL GLDNAGKTTL
MKKFLDEPTD TIEPTLGFDI KTVTFKGFQL NLWDVGGQKS LRSYWKNYFE STDALIWVVD
SSDRERLTQC SEELKKLLGE ERLAGASLLV LANKSDLPGA IDVNSIAQVL DLQSIKSHHW
KIFSCCALSG DRLIQAMTWL CDDVGSRIFI LD
//
