ID   IF1A_THEVO              Reviewed;         123 AA.
AC   Q979F7;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 103.
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; OrderedLocusNames=TV1204; ORFNames=TVG1232812;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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; BA000011; BAB60346.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q979F7; -.
DR   SMR; Q979F7; -.
DR   STRING; 273116.14325442; -.
DR   EnsemblBacteria; BAB60346; BAB60346; BAB60346.
DR   KEGG; tvo:TVG1232812; -.
DR   eggNOG; arCOG01179; Archaea.
DR   HOGENOM; CLU_109098_1_2_2; -.
DR   OMA; VPWDFQD; -.
DR   PhylomeDB; Q979F7; -.
DR   Proteomes; UP000001017; 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.
FT   CHAIN           1..123
FT                   /note="Translation initiation factor 1A"
FT                   /id="PRO_0000145137"
FT   DOMAIN          28..102
FT                   /note="S1-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00216"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   123 AA;  14531 MW;  D08E08B0B71C53F6 CRC64;
     MSPDKTEDED KDVNVDQDQF NEEEESLGRV ILPNKKKGEM FGIVEKMEGA SRLSVMCEDG
     YTRNARIPGR MRKRMWIREK DLVIVKPWEF QPEKADVVYR YTKTQASYLS RNHMLPEVID
     IFK