ID   IF1A_SULAC              Reviewed;         108 AA.
AC   Q4JA54;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Translation initiation factor 1A {ECO:0000255|HAMAP-Rule:MF_00216};
DE            Short=aIF-1A {ECO:0000255|HAMAP-Rule:MF_00216};
GN   Name=eif1a {ECO:0000255|HAMAP-Rule:MF_00216}; OrderedLocusNames=Saci_0964;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- FUNCTION: Seems to be required for maximal rate of protein
CC       biosynthesis. Enhances ribosome dissociation into subunits and
CC       stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_00216}.
CC   -!- SIMILARITY: Belongs to the eIF-1A family. {ECO:0000255|HAMAP-
CC       Rule:MF_00216}.
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DR   EMBL; CP000077; AAY80326.1; -; Genomic_DNA.
DR   RefSeq; WP_011277828.1; NC_007181.1.
DR   AlphaFoldDB; Q4JA54; -.
DR   SMR; Q4JA54; -.
DR   STRING; 330779.Saci_0964; -.
DR   EnsemblBacteria; AAY80326; AAY80326; Saci_0964.
DR   GeneID; 3472906; -.
DR   KEGG; sai:Saci_0964; -.
DR   PATRIC; fig|330779.12.peg.925; -.
DR   eggNOG; arCOG01179; Archaea.
DR   HOGENOM; CLU_109098_1_2_2; -.
DR   OMA; ADITWRY; -.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd05793; S1_IF1A; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00216; aIF_1A; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR   InterPro; IPR001253; TIF_eIF-1A.
DR   InterPro; IPR018104; TIF_eIF-1A_CS.
DR   PANTHER; PTHR21668; PTHR21668; 1.
DR   Pfam; PF01176; eIF-1a; 1.
DR   SMART; SM00652; eIF1a; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00523; eIF-1A; 1.
DR   PROSITE; PS01262; IF1A; 1.
DR   PROSITE; PS50832; S1_IF1_TYPE; 1.
PE   3: Inferred from homology;
KW   Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..108
FT                   /note="Translation initiation factor 1A"
FT                   /id="PRO_0000145133"
FT   DOMAIN          11..85
FT                   /note="S1-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00216"
SQ   SEQUENCE   108 AA;  12376 MW;  939D0B4D9ECE3CD3 CRC64;
     MAKKKSNTEQ PTREVVKPIE GEVICVVKKL FGGEHVQVIC TDGKERLGRI PGKLKKKVWI
     REGDVVLAAP WDFQPNKCDI VYRYTESEVR RLVEDKVISQ DVIEQLRG