IF2A_THEGJ
ID IF2A_THEGJ Reviewed; 273 AA.
AC C5A4Z9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=TGAM_0809;
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
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; CP001398; ACS33311.1; -; Genomic_DNA.
DR RefSeq; WP_014121321.1; NC_012804.1.
DR AlphaFoldDB; C5A4Z9; -.
DR SMR; C5A4Z9; -.
DR STRING; 593117.TGAM_0809; -.
DR PaxDb; C5A4Z9; -.
DR EnsemblBacteria; ACS33311; ACS33311; TGAM_0809.
DR GeneID; 7988976; -.
DR KEGG; tga:TGAM_0809; -.
DR PATRIC; fig|593117.10.peg.806; -.
DR eggNOG; arCOG04107; Archaea.
DR HOGENOM; CLU_033458_0_2_2; -.
DR OMA; DVNEHQR; -.
DR OrthoDB; 84684at2157; -.
DR Proteomes; UP000001488; 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..273
FT /note="Translation initiation factor 2 subunit alpha"
FT /id="PRO_1000204376"
FT DOMAIN 12..83
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00231"
SQ SEQUENCE 273 AA; 31549 MW; 236609EF954C6700 CRC64;
MPRKAREYPE EGEFVVATVK NIHPYGAFLI LDEYPGKEGF MHISEVAPTW VKNIRDYVKE
GQKVVVKVIR VDPEKGHIDL SLKRVNQQQR KAKLQEYKRA QKAENLLKMA AEKIGKDFET
AWREVWVPLE EEYGEVYAAF EDAAQNGIEV LKGLIPDEWL DALKPIIEAY VEIPTVTIDA
EFEITVPKPN GIEIIKEALI RARDRANEEK DIDVKFTYQG APRYRIDITA PDYYKAEEVL
ESIAEEILRV IKEAGGEATL IRKEKRIRKI KRR
