ID   IF2A_HALS3              Reviewed;         267 AA.
AC   B0R3M0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Translation initiation factor 2 subunit alpha {ECO:0000255|HAMAP-Rule:MF_00231};
DE   AltName: Full=aIF2-alpha {ECO:0000255|HAMAP-Rule:MF_00231};
DE   AltName: Full=eIF-2-alpha {ECO:0000255|HAMAP-Rule:MF_00231};
GN   Name=eif2a {ECO:0000255|HAMAP-Rule:MF_00231}; OrderedLocusNames=OE_1818R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
CC   -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis by
CC       forming a ternary complex with GTP and initiator tRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_00231}.
CC   -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC       {ECO:0000255|HAMAP-Rule:MF_00231}.
CC   -!- SIMILARITY: Belongs to the eIF-2-alpha family. {ECO:0000255|HAMAP-
CC       Rule:MF_00231}.
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DR   EMBL; AM774415; CAP13334.1; -; Genomic_DNA.
DR   RefSeq; WP_010902366.1; NC_010364.1.
DR   AlphaFoldDB; B0R3M0; -.
DR   SMR; B0R3M0; -.
DR   EnsemblBacteria; CAP13334; CAP13334; OE_1818R.
DR   GeneID; 5954024; -.
DR   GeneID; 62886187; -.
DR   KEGG; hsl:OE_1818R; -.
DR   HOGENOM; CLU_033458_0_2_2; -.
DR   OMA; DVNEHQR; -.
DR   PhylomeDB; B0R3M0; -.
DR   Proteomes; UP000001321; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd04452; S1_IF2_alpha; 1.
DR   Gene3D; 1.10.150.190; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.70.1130; -; 1.
DR   HAMAP; MF_00231; eIF_2_alpha; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   InterPro; IPR044126; S1_IF2_alpha.
DR   InterPro; IPR022964; TIF2_asu_arc.
DR   InterPro; IPR024055; TIF2_asu_C.
DR   InterPro; IPR024054; TIF2_asu_middle_sf.
DR   InterPro; IPR011488; TIF_2_asu.
DR   PANTHER; PTHR10602; PTHR10602; 1.
DR   Pfam; PF07541; EIF_2_alpha; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF110993; SSF110993; 1.
DR   SUPFAM; SSF116742; SSF116742; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Initiation factor; Protein biosynthesis; RNA-binding.
FT   CHAIN           1..267
FT                   /note="Translation initiation factor 2 subunit alpha"
FT                   /id="PRO_1000100484"
FT   DOMAIN          10..81
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00231"
SQ   SEQUENCE   267 AA;  29336 MW;  691EB38E39422A07 CRC64;
     MKYEGWPDEG ELVVGKVDDI EDFGVFVDLE QYQDKRGLVH VSEVASGWIK NVRDHVNEDQ
     TVVAKVLGVD ESAQQIDLSL KDVNDHQHSD TIQEWKNEQK ADKWLTLAFG EDMADDQFRR
     IANGLLADFG SLYDGFEQAA IHGHEALADT ALEDDEIDAI VETARDNVSV PYVTVTGYVS
     LQSPDGDGVD TIKDALQAAE GNGEVPDEVD LDVTYVGAPE YRLRVQAPNY KTAESALEAA
     GDRAVDSVTA HDGSGAFHRE RQLDDDA