ID   IF2A_AERPE              Reviewed;         277 AA.
AC   Q9YF02;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2002, sequence version 3.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Translation initiation factor 2 subunit alpha;
DE   AltName: Full=aIF2-alpha;
DE   AltName: Full=eIF-2-alpha;
GN   Name=eif2a; OrderedLocusNames=APE_0436.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
CC   -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis by
CC       forming a ternary complex with GTP and initiator tRNA. {ECO:0000250}.
CC   -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eIF-2-alpha family. {ECO:0000305}.
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DR   EMBL; BA000002; BAA79394.2; -; Genomic_DNA.
DR   PIR; F72737; F72737.
DR   AlphaFoldDB; Q9YF02; -.
DR   SMR; Q9YF02; -.
DR   STRING; 272557.APE_0436.1; -.
DR   EnsemblBacteria; BAA79394; BAA79394; APE_0436.1.
DR   KEGG; ape:APE_0436.1; -.
DR   PATRIC; fig|272557.25.peg.325; -.
DR   eggNOG; arCOG04107; Archaea.
DR   OMA; DVNEHQR; -.
DR   Proteomes; UP000002518; 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; Reference proteome; RNA-binding.
FT   CHAIN           1..277
FT                   /note="Translation initiation factor 2 subunit alpha"
FT                   /id="PRO_0000137390"
FT   DOMAIN          22..93
FT                   /note="S1 motif"
SQ   SEQUENCE   277 AA;  31479 MW;  F227C70657AEAAD0 CRC64;
     MSEEGGVEVK LLKPRKPLPD VGEIVVGTVQ EVHDYGAYLI LDEYGGVRAF LPWSEIASRA
     VRNIHAVLKP RQKVVVKVIR VYKKRGQVDV SLKRVMDSEK KRKMMFYKRY LKAATLVELI
     AEKLGKSVDE AYREVLWKLE DAYGDPMKGL EAAVLQGREA LEKAGVPEEW IEPLLETAKT
     HVRVKTVKIT FYLTLRSMAG DGVERVRKVL EAAKSQIESF KDSKVVARIY TVGAPKYRVE
     LQGYNYKTLE KALEKMVEAA RKTASKLGVE FSFERED