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Database: UniProt
Entry: A0A2I8VMH1_9EURY
LinkDB: A0A2I8VMH1_9EURY
Original site: A0A2I8VMH1_9EURY 
ID   A0A2I8VMH1_9EURY        Unreviewed;        94 AA.
AC   A0A2I8VMH1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Translation initiation factor 1A {ECO:0000256|HAMAP-Rule:MF_00216};
DE            Short=aIF-1A {ECO:0000256|HAMAP-Rule:MF_00216};
GN   Name=eif1A {ECO:0000313|EMBL:AUV83126.1};
GN   Synonyms=eif1a {ECO:0000256|HAMAP-Rule:MF_00216};
GN   ORFNames=C2R22_16955 {ECO:0000313|EMBL:AUV83126.1};
OS   Salinigranum rubrum.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Salinigranum.
OX   NCBI_TaxID=755307 {ECO:0000313|EMBL:AUV83126.1, ECO:0000313|Proteomes:UP000236584};
RN   [1] {ECO:0000313|EMBL:AUV83126.1, ECO:0000313|Proteomes:UP000236584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GX10 {ECO:0000313|EMBL:AUV83126.1,
RC   ECO:0000313|Proteomes:UP000236584};
RA   Han S.;
RT   "Complete genome sequence of Salinigranum rubrum GX10T, an extremely
RT   halophilic archaeon isolated from a marine solar saltern.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00025502, ECO:0000256|HAMAP-
CC       Rule:MF_00216, ECO:0000256|RuleBase:RU004365}.
CC   -!- SIMILARITY: Belongs to the eIF-1A family.
CC       {ECO:0000256|ARBA:ARBA00007392, ECO:0000256|HAMAP-Rule:MF_00216,
CC       ECO:0000256|RuleBase:RU004364}.
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DR   EMBL; CP026309; AUV83126.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I8VMH1; -.
DR   KEGG; srub:C2R22_16955; -.
DR   OrthoDB; 2586at2157; -.
DR   Proteomes; UP000236584; 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; Nucleic acid-binding proteins; 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   NCBIfam; TIGR00523; eIF-1A; 1.
DR   PANTHER; PTHR21668; EIF-1A; 1.
DR   PANTHER; PTHR21668:SF30; TRANSLATION INITIATION FACTOR 1A 2; 1.
DR   Pfam; PF01176; eIF-1a; 1.
DR   SMART; SM00652; eIF1a; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS01262; IF1A; 1.
DR   PROSITE; PS50832; S1_IF1_TYPE; 1.
PE   3: Inferred from homology;
KW   Initiation factor {ECO:0000256|HAMAP-Rule:MF_00216, ECO:0000256|PROSITE-
KW   ProRule:PRU00181};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00216, ECO:0000256|PROSITE-
KW   ProRule:PRU00181}; Reference proteome {ECO:0000313|Proteomes:UP000236584}.
FT   DOMAIN          6..80
FT                   /note="S1-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50832"
SQ   SEQUENCE   94 AA;  11095 MW;  61C299D028E4C797 CRC64;
     MSEEVERKNL RMPNGSELFA VVTEHNGGNH VRVRCEDGKN RMGRIPGRMK YRTWINEGDV
     VLVEPWDWQD EKANIEWRYS GQDADQLRRE GHID
//
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