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IF1A_SULTO
ID   IF1A_SULTO              Reviewed;         108 AA.
AC   Q974Z9; F9VN17;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Translation initiation factor 1A;
DE            Short=aIF-1A;
GN   Name=eIF1A; OrderedLocusNames=STK_05135; ORFNames=STS070;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eIF-1A family. {ECO:0000305}.
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DR   EMBL; BA000023; BAK54314.1; -; Genomic_DNA.
DR   RefSeq; WP_052846355.1; NC_003106.2.
DR   AlphaFoldDB; Q974Z9; -.
DR   SMR; Q974Z9; -.
DR   STRING; 273063.STK_05135; -.
DR   EnsemblBacteria; BAK54314; BAK54314; STK_05135.
DR   GeneID; 42800061; -.
DR   KEGG; sto:STK_05135; -.
DR   PATRIC; fig|273063.9.peg.591; -.
DR   eggNOG; arCOG01179; Archaea.
DR   OMA; ADITWRY; -.
DR   OrthoDB; 102432at2157; -.
DR   Proteomes; UP000001015; 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_0000145135"
FT   DOMAIN          11..85
FT                   /note="S1-like"
SQ   SEQUENCE   108 AA;  12279 MW;  B8D0C734AF3FD130 CRC64;
     MAKKKTNEQP SVKEVPKPAE GEVICVVKKM LGAEHVQVIC LDGKERLGRI PGKMKKKMWV
     KEGDVVLAAP WDFQPNKCDI IYKYSESEVR RLEEEQVVSA DIIEQLRG
 
 
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