ID   IF1A_PICTO              Reviewed;         108 AA.
AC   Q6L2G4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=PTO0253;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017261; AAT42838.1; -; Genomic_DNA.
DR   RefSeq; WP_011177054.1; NC_005877.1.
DR   AlphaFoldDB; Q6L2G4; -.
DR   SMR; Q6L2G4; -.
DR   STRING; 263820.PTO0253; -.
DR   EnsemblBacteria; AAT42838; AAT42838; PTO0253.
DR   GeneID; 2844146; -.
DR   KEGG; pto:PTO0253; -.
DR   PATRIC; fig|263820.9.peg.271; -.
DR   eggNOG; arCOG01179; Archaea.
DR   HOGENOM; CLU_109098_1_2_2; -.
DR   OMA; ADITWRY; -.
DR   OrthoDB; 102432at2157; -.
DR   Proteomes; UP000000438; 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_0000145127"
FT   DOMAIN          10..84
FT                   /note="S1-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00216"
SQ   SEQUENCE   108 AA;  12625 MW;  0095751A081761B8 CRC64;
     MDNDNDENTI RVITPNKKSG EIYGIVEKMS GASRLIVMCE DGVTRNCRIP GKMKKRMWIR
     EGDLVIVKPW EFQDEKGDII YRYTKTQAAY LSRNHMLPEI IDVFNEKQ