ID   IF2A_PYRAE              Reviewed;         265 AA.
AC   Q8ZTY5;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=PAE3032;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64624.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZTY5; -.
DR   SMR; Q8ZTY5; -.
DR   STRING; 178306.PAE3032; -.
DR   EnsemblBacteria; AAL64624; AAL64624; PAE3032.
DR   KEGG; pai:PAE3032; -.
DR   PATRIC; fig|178306.9.peg.2281; -.
DR   eggNOG; arCOG04107; Archaea.
DR   HOGENOM; CLU_033458_0_2_2; -.
DR   InParanoid; Q8ZTY5; -.
DR   OMA; DVNEHQR; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
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; Reference proteome; RNA-binding.
FT   CHAIN           1..265
FT                   /note="Translation initiation factor 2 subunit alpha"
FT                   /id="PRO_0000137398"
FT   DOMAIN          12..82
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00231"
SQ   SEQUENCE   265 AA;  30561 MW;  DE714B5B27D91A20 CRC64;
     MRLVKKEFPD VGELVIGTVK KIAEHGAYVY LDEYDLEAFA PTQEIVQSWF HSIRDYVKEG
     NKTVFKVISV NPKMRVVEVS LKRVRVDEKE KKLLLYRHRV RVLKLLEIAM KKLNRPAEEA
     LKVMWYLEEQ FGDPFKVFEE VVKTGPHVLD DLQLDAKLKE IIIELARQQV ELPPTKISGI
     IKIVSVEGDG VEKIKAALIE LEKTLREKFP QISTKIYVVG PPRYRIDLTG QQPKQVEAAF
     SEAANILQAL QKKYKVIGNI QRIEQ