ID A0A218NZR9_THECE Unreviewed; 275 AA.
AC A0A218NZR9;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Translation initiation factor 2 subunit alpha {ECO:0000256|ARBA:ARBA00013678, ECO:0000256|HAMAP-Rule:MF_00231};
DE AltName: Full=aIF2-alpha {ECO:0000256|ARBA:ARBA00030860, ECO:0000256|HAMAP-Rule:MF_00231};
DE AltName: Full=eIF-2-alpha {ECO:0000256|ARBA:ARBA00033333, ECO:0000256|HAMAP-Rule:MF_00231};
GN Name=eif2a {ECO:0000256|HAMAP-Rule:MF_00231};
GN ORFNames=A3L02_00585 {ECO:0000313|EMBL:ASI98171.1};
OS Thermococcus celer Vu 13 = JCM 8558.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=1293037 {ECO:0000313|EMBL:ASI98171.1, ECO:0000313|Proteomes:UP000197156};
RN [1] {ECO:0000313|EMBL:ASI98171.1, ECO:0000313|Proteomes:UP000197156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vu 13 {ECO:0000313|EMBL:ASI98171.1,
RC ECO:0000313|Proteomes:UP000197156};
RA Oger P.M.;
RT "Complete genome sequence of Thermococcus celer.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00003323, ECO:0000256|HAMAP-Rule:MF_00231}.
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC {ECO:0000256|ARBA:ARBA00011243, ECO:0000256|HAMAP-Rule:MF_00231}.
CC -!- SIMILARITY: Belongs to the eIF-2-alpha family.
CC {ECO:0000256|ARBA:ARBA00007223, ECO:0000256|HAMAP-Rule:MF_00231}.
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DR EMBL; CP014854; ASI98171.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218NZR9; -.
DR KEGG; tce:A3L02_00585; -.
DR OrthoDB; 84794at2157; -.
DR Proteomes; UP000197156; 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; 3.30.70.1130; EIF_2_alpha; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_00231; eIF_2_alpha; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1; 1.
DR PANTHER; PTHR10602:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1; 1.
DR Pfam; PF07541; EIF_2_alpha; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF110993; eIF-2-alpha, C-terminal domain; 1.
DR SUPFAM; SSF116742; eIF2alpha middle domain-like; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00231};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00231};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00231}.
FT DOMAIN 12..83
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT COILED 192..253
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 275 AA; 31716 MW; A3EFF8FE7273C414 CRC64;
MPRKAKEYPE EGEFVVATVK NIHHYGAFLK LDEYPGKEGF MHISEVASTW VKNIRDYIKE
GQKIVAKVIR VDPSKGHIDL SLKRVNQQQR KAKLQEYKRA QKAENLLKMA AEKMGKDFET
AWREVWVPLE EEYGEVYAAF EDAAQNGMDV LKGLISDEWI EALKPIIEAY VEIPTVTIDA
EFEITVPTSN GIETIKEALI RARDRANEEK EIEVRFSYQG APRYRIDITA PDYHRAEEVL
EEVADEILRV IKEAGGEATL IRKEKRIKKI KRRGQ
//