ID   IF1A_HALMA              Reviewed;          95 AA.
AC   Q5UZM2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 85.
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=rrnAC2474;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(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   -!- SEQUENCE CAUTION:
CC       Sequence=AAV47281.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AY596297; AAV47281.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004516096.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5UZM2; -.
DR   SMR; Q5UZM2; -.
DR   STRING; 272569.rrnAC2474; -.
DR   EnsemblBacteria; AAV47281; AAV47281; rrnAC2474.
DR   GeneID; 40153370; -.
DR   GeneID; 64824277; -.
DR   KEGG; hma:rrnAC2474; -.
DR   PATRIC; fig|272569.17.peg.3086; -.
DR   eggNOG; arCOG01179; Archaea.
DR   HOGENOM; CLU_109098_1_2_2; -.
DR   Proteomes; UP000001169; Chromosome I.
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..95
FT                   /note="Translation initiation factor 1A"
FT                   /id="PRO_0000259363"
FT   DOMAIN          6..80
FT                   /note="S1-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00216"
SQ   SEQUENCE   95 AA;  11378 MW;  AAB4463DF346707E CRC64;
     MSDNDSRKNL RMPEEDEVFA VVMDMLGANR VKVRCMDGVE RTARIPGKMQ KRIWIREDDV
     VLVEPWDWQD EKADITWRYE KQDADQLREE GHIQE