ID   IF2A_HALMA              Reviewed;         266 AA.
AC   Q5UX22;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=rrnAC3512;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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; AY596297; AAV48181.1; -; Genomic_DNA.
DR   RefSeq; WP_004963592.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5UX22; -.
DR   SMR; Q5UX22; -.
DR   STRING; 272569.rrnAC3512; -.
DR   EnsemblBacteria; AAV48181; AAV48181; rrnAC3512.
DR   GeneID; 40154283; -.
DR   GeneID; 64823266; -.
DR   KEGG; hma:rrnAC3512; -.
DR   PATRIC; fig|272569.17.peg.4018; -.
DR   eggNOG; arCOG04107; Archaea.
DR   HOGENOM; CLU_033458_0_2_2; -.
DR   OMA; DVNEHQR; -.
DR   Proteomes; UP000001169; Chromosome I.
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; Reference proteome; RNA-binding.
FT   CHAIN           1..266
FT                   /note="Translation initiation factor 2 subunit alpha"
FT                   /id="PRO_0000137392"
FT   DOMAIN          10..81
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00231"
FT   REGION          233..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   266 AA;  29614 MW;  EA9954E37BC20848 CRC64;
     MKYSGWPEPG ELVVGKIDEI EDFGVFVDLD EYEGKRGLCH ISEVASGWIK NVRDHVNEGQ
     TVVAKVLDVD ESAQQIDLSI KDVNDHQRKE KIQEWKNEQK ADNWMELAFG EDLDDETYAA
     IANELLAEFG SMYDGFESAA IHGKDALEDV DLSEEEIDAI VQTARNNVSV PYVQVTGYVD
     LSCPESDGVD IIKEALQAAE GNGEVPDEIE LEVTYVGSPE YRIQVQAPDY KTAEDALEES
     ADRAAKVVEQ HGGSGQFHRE RSEDDE