ID   IF1A_PYRHO              Reviewed;         115 AA.
AC   O59280;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Translation initiation factor 1A;
DE            Short=aIF-1A;
GN   Name=eIF1A; OrderedLocusNames=PH1568;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA30680.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000001; BAA30680.1; ALT_INIT; Genomic_DNA.
DR   PIR; H71034; H71034.
DR   AlphaFoldDB; O59280; -.
DR   SMR; O59280; -.
DR   STRING; 70601.3257997; -.
DR   EnsemblBacteria; BAA30680; BAA30680; BAA30680.
DR   KEGG; pho:PH1568; -.
DR   eggNOG; arCOG01179; Archaea.
DR   OMA; ADITWRY; -.
DR   Proteomes; UP000000752; 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..115
FT                   /note="Translation initiation factor 1A"
FT                   /id="PRO_0000145131"
FT   DOMAIN          14..89
FT                   /note="S1-like"
SQ   SEQUENCE   115 AA;  13316 MW;  C03AC130D24EB221 CRC64;
     MIMPKKERKV EGEEVIRVPL PEGNQLFGVV EQALGAGWMD VRCEDGKIRR CRIPGKLRRR
     VWIRVGDLVI VQPWPVQSDK RGDIVYRYTQ TQVDWLLRKG KITQEFLTGG SLLVE