ID   IF2A_PYRFU              Reviewed;         275 AA.
AC   Q8U1R5;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=PF1140;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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; AE009950; AAL81264.1; -; Genomic_DNA.
DR   RefSeq; WP_011012280.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U1R5; -.
DR   SMR; Q8U1R5; -.
DR   IntAct; Q8U1R5; 1.
DR   STRING; 186497.PF1140; -.
DR   EnsemblBacteria; AAL81264; AAL81264; PF1140.
DR   GeneID; 41712949; -.
DR   KEGG; pfu:PF1140; -.
DR   PATRIC; fig|186497.12.peg.1201; -.
DR   eggNOG; arCOG04107; Archaea.
DR   HOGENOM; CLU_033458_0_2_2; -.
DR   OMA; DVNEHQR; -.
DR   OrthoDB; 84684at2157; -.
DR   PhylomeDB; Q8U1R5; -.
DR   Proteomes; UP000001013; 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..275
FT                   /note="Translation initiation factor 2 subunit alpha"
FT                   /id="PRO_0000137399"
FT   DOMAIN          12..83
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00231"
SQ   SEQUENCE   275 AA;  31917 MW;  1AEE323D1DC5F8FF CRC64;
     MPRRAREYPE EGELVVATVK RVHNYGAFLD LDEYPGKEGF MHISEVASTW VKNIRDYLRE
     GQKVVAKVIR VDPKKGHIDL SLRRVTQQQR KAKLQEFKRA QKAENLLKLA AEKLGKDFEE
     AWREVWVPLE NEWGEVYAAF EDAARNGIEV LKGYVPDEWL PVLKEIIDSY VEVPTVTIDA
     EFEITVPKPN GIEIIKEALI KARDRANQEK DIEVKFTYLG APRYRIDITA PDYYKAEEVL
     EDIAEEILRV IKEAGGEATL LRKEKRIRKV KKRKK