ID Q95XR0_CAEEL Unreviewed; 469 AA.
AC Q95XR0;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 163.
DE RecName: Full=protein-synthesizing GTPase {ECO:0000256|ARBA:ARBA00011986};
DE EC=3.6.5.3 {ECO:0000256|ARBA:ARBA00011986};
GN Name=eif-2gamma {ECO:0000313|EMBL:CCD69906.1,
GN ECO:0000313|WormBase:Y39G10AR.8};
GN ORFNames=CELE_Y39G10AR.8 {ECO:0000313|EMBL:CCD69906.1}, Y39G10AR.8
GN {ECO:0000313|WormBase:Y39G10AR.8};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD69906.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD69906.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD69906.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001874};
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DR EMBL; BX284601; CCD69906.1; -; Genomic_DNA.
DR RefSeq; NP_490960.1; NM_058559.6.
DR AlphaFoldDB; Q95XR0; -.
DR SMR; Q95XR0; -.
DR DIP; DIP-24612N; -.
DR IntAct; Q95XR0; 2.
DR STRING; 6239.Y39G10AR.8.1; -.
DR EPD; Q95XR0; -.
DR PaxDb; 6239-Y39G10AR-8; -.
DR PeptideAtlas; Q95XR0; -.
DR EnsemblMetazoa; Y39G10AR.8.1; Y39G10AR.8.1; WBGene00021466.
DR GeneID; 171792; -.
DR KEGG; cel:CELE_Y39G10AR.8; -.
DR UCSC; Y39G10AR.8; c. elegans.
DR AGR; WB:WBGene00021466; -.
DR WormBase; Y39G10AR.8; CE27254; WBGene00021466; eif-2gamma.
DR eggNOG; KOG0466; Eukaryota.
DR GeneTree; ENSGT00940000172475; -.
DR HOGENOM; CLU_027154_0_1_1; -.
DR InParanoid; Q95XR0; -.
DR OMA; NIGMVGH; -.
DR OrthoDB; 1512042at2759; -.
DR PhylomeDB; Q95XR0; -.
DR Reactome; R-CEL-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-CEL-381042; PERK regulates gene expression.
DR Reactome; R-CEL-382556; ABC-family proteins mediated transport.
DR Reactome; R-CEL-72649; Translation initiation complex formation.
DR Reactome; R-CEL-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-CEL-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-CEL-72731; Recycling of eIF2:GDP.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00021466; Expressed in adult organism and 4 other cell types or tissues.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR CDD; cd01888; eIF2_gamma; 1.
DR CDD; cd03688; eIF2_gamma_II; 1.
DR CDD; cd15490; eIF2_gamma_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015256; eIF2g_C.
DR InterPro; IPR044127; eIF2g_dom_2.
DR InterPro; IPR044128; eIF2g_GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR PANTHER; PTHR42854; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3 FAMILY MEMBER; 1.
DR PANTHER; PTHR42854:SF3; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3-RELATED; 1.
DR Pfam; PF09173; eIF2_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Proteomics identification {ECO:0007829|EPD:Q95XR0,
KW ECO:0007829|PeptideAtlas:Q95XR0};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT DOMAIN 38..246
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 469 AA; 51234 MW; BF7DBF8ECCE7B748 CRC64;
MASEAEKDKC QSWLAKQDLD KVGVDNLNPL TEEVISRQAT INIGTIGHVA HGKSTLVKAF
SGVHTVKFKR ELERNITIKL GYANAKIYRC SNQECPRPGC YRSAGSSTPD RFPCERAGCG
GEFTCVRHVS FVDCPGHDIL MATMLNGAAV MDAAFLLVAG NEPCPQPQTS EHLAAVEIMQ
LNHLMILQNK VDIIKESQAR ENYEQIAGFV QGTVAENAPV IPISAQLKYN VDLVCEYLCK
KIPVPVRDFK SPARLIIIRS FDVNKPGSEV ENLKGGVAGG TLTKGILRVG QEIEVRPGIV
SKTATGQLQC RPIFSRIDSL FAEKNQLEYA VPGGLIGVGT KIDPTLCRGD RLVGHILGAV
GTLPDIFIEI EISFYLLRRL LGVRTEGKKK GAKVQKLVKE ETLLVNIGSL STGGRVTAVK
GDAAKIRLND PICTEVGEKI AMSRRFEKSW RLIGWGTIRK GQTVEPYKN
//
