ID   IF1A_PYRFU              Reviewed;         115 AA.
AC   Q8U0K5;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 105.
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=PF1582;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAL81706.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE009950; AAL81706.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8U0K5; -.
DR   SMR; Q8U0K5; -.
DR   STRING; 186497.PF1582; -.
DR   PRIDE; Q8U0K5; -.
DR   EnsemblBacteria; AAL81706; AAL81706; PF1582.
DR   KEGG; pfu:PF1582; -.
DR   PATRIC; fig|186497.12.peg.1648; -.
DR   eggNOG; arCOG01179; Archaea.
DR   HOGENOM; CLU_109098_1_2_2; -.
DR   OMA; ADITWRY; -.
DR   PhylomeDB; Q8U0K5; -.
DR   Proteomes; UP000001013; 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..115
FT                   /note="Translation initiation factor 1A"
FT                   /id="PRO_0000145130"
FT   DOMAIN          14..89
FT                   /note="S1-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00216"
SQ   SEQUENCE   115 AA;  13317 MW;  532CFA53EE417551 CRC64;
     MLMPKKERKV EGEEVIRVPL PEGNQLFGVV EQALGAGWMD VRCEDGKVRR CRIPGRLRRR
     VWIKVGDLVI VEPWPVQSDK RGDIVYRYTQ TQVEWLLRKG KISQEFLTGG SLLLE