ID D2PJK3_SULID Unreviewed; 266 AA.
AC D2PJK3;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 OrderedLocusNames=LD85_1285 {ECO:0000313|EMBL:ADB86956.1};
OS Sulfolobus islandicus (strain L.D.8.5 / Lassen #2).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=425944 {ECO:0000313|EMBL:ADB86956.1, ECO:0000313|Proteomes:UP000001404};
RN [1] {ECO:0000313|Proteomes:UP000001404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L.D.8.5 / Lassen #2 {ECO:0000313|Proteomes:UP000001404};
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001731; ADB86956.1; -; Genomic_DNA.
DR RefSeq; WP_012952790.1; NC_013769.1.
DR AlphaFoldDB; D2PJK3; -.
DR GeneID; 8761099; -.
DR KEGG; sii:LD85_1285; -.
DR HOGENOM; CLU_033458_0_2_2; -.
DR Proteomes; UP000001404; 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 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"
SQ SEQUENCE 266 AA; 30342 MW; E5BA69FB7EB57C68 CRC64;
MIYSRSRLPS EGEILIATVK QVFDYGSYIT LDEYGGLQAF LPWSEVSSKW VKNIRDVLKE
NRKVVVKVIR VDRRKGAVDV SLKKVTDDER RKKNLQWKKI QRLDKILELV SQQLKLSEKD
AWEQVAWKLE AKYGDPISAI ERAVKEGEKI LIDAGVPEIW IKPLLEEAAK HTEEKKVKMS
GLITVKTSEP LGVQKIKEVM SKALENIEQD YESILNVKIY TIGAPRYRVD VVGTNPKDAS
EALNQIISNL IKIGKEENVD ISVVKK
//
