ID   IF2A_THEON              Reviewed;         275 AA.
AC   B6YT35;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=TON_0237;
OS   Thermococcus onnurineus (strain NA1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1;
RX   PubMed=18790866; DOI=10.1128/jb.00746-08;
RA   Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA   Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA   Colwell R.R., Kim S.-J., Lee J.-H.;
RT   "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT   mixed heterotrophic and carboxydotrophic metabolism.";
RL   J. Bacteriol. 190:7491-7499(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; CP000855; ACJ15722.1; -; Genomic_DNA.
DR   RefSeq; WP_012571195.1; NC_011529.1.
DR   AlphaFoldDB; B6YT35; -.
DR   SMR; B6YT35; -.
DR   STRING; 523850.TON_0237; -.
DR   EnsemblBacteria; ACJ15722; ACJ15722; TON_0237.
DR   GeneID; 7017899; -.
DR   KEGG; ton:TON_0237; -.
DR   PATRIC; fig|523850.10.peg.239; -.
DR   eggNOG; arCOG04107; Archaea.
DR   HOGENOM; CLU_033458_0_2_2; -.
DR   OMA; DVNEHQR; -.
DR   OrthoDB; 84684at2157; -.
DR   Proteomes; UP000002727; 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..275
FT                   /note="Translation initiation factor 2 subunit alpha"
FT                   /id="PRO_1000100485"
FT   DOMAIN          12..83
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00231"
SQ   SEQUENCE   275 AA;  31713 MW;  31952309DDFB052D CRC64;
     MPRKAKEYPE EGEFVIATVK SIHPYGAFLK LDEYPGKEGF MHISEVASTW VKNIRDYVKE
     GQKVVAKVIR VDPNKGHIDL SLKRVNQQQR KAKLQEYKRA QKAENLLKMA AEKLGKDFEM
     AWQEVWVPLE EEYGEVYAAF EDAAQNGIEV LKGIIPEEWL EPLNEIVQNY VEVPTVTIDA
     EFEITVPKPN GIEIIKEALI RARDRVNEDK DIEVKFTYQG APRYRIDITA PDYYKAEEVL
     EDIAEEILRV IKQAGGEATL LRKEKRIKKI KRRGA