IF2A_THEKO
ID IF2A_THEKO Reviewed; 275 AA.
AC Q5JE49;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=TK1100;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AP006878; BAD85289.1; -; Genomic_DNA.
DR RefSeq; WP_011250051.1; NC_006624.1.
DR AlphaFoldDB; Q5JE49; -.
DR SMR; Q5JE49; -.
DR STRING; 69014.TK1100; -.
DR PRIDE; Q5JE49; -.
DR EnsemblBacteria; BAD85289; BAD85289; TK1100.
DR GeneID; 3233948; -.
DR KEGG; tko:TK1100; -.
DR PATRIC; fig|69014.16.peg.1076; -.
DR eggNOG; arCOG04107; Archaea.
DR HOGENOM; CLU_033458_0_2_2; -.
DR InParanoid; Q5JE49; -.
DR OMA; DVNEHQR; -.
DR OrthoDB; 84684at2157; -.
DR PhylomeDB; Q5JE49; -.
DR Proteomes; UP000000536; 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..275
FT /note="Translation initiation factor 2 subunit alpha"
FT /id="PRO_0000137401"
FT DOMAIN 12..83
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00231"
SQ SEQUENCE 275 AA; 31590 MW; 52C9A8448C6DB0E3 CRC64;
MPRKAKEYPE EGEFVVATVK NIHPYGAFLT LDEYPGKEGF MHISEVAPTW VKNIRDYLKE
GQKIVAKVIR VDPEKGHIDL SLKRVNQQQR KAKLQEYKRA QKAENLLKMA AEKLGKDFET
AWREVWVPLE EEYGEVYAAF EDAAQNGMDV LKGLISDEWI EALKPIIEAY VEIPTVTIDA
EFEITVPKPN GIEIIKEALI KARDRANQEK DIEVKFSYQG APRYRIDITA PDYYKAEEVL
EDIAEEILRV IKEAGGEATL IRKEKRIKKV KKRGS
