ID N0BDR4_9EURY Unreviewed; 78 AA.
AC N0BDR4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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:0000256|HAMAP-Rule:MF_00216};
GN ORFNames=Asulf_00348 {ECO:0000313|EMBL:AGK60377.1};
OS Archaeoglobus sulfaticallidus PM70-1.
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=387631 {ECO:0000313|EMBL:AGK60377.1, ECO:0000313|Proteomes:UP000013307};
RN [1] {ECO:0000313|EMBL:AGK60377.1, ECO:0000313|Proteomes:UP000013307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM70-1 {ECO:0000313|EMBL:AGK60377.1};
RX PubMed=23833130;
RA Stokke R., Hocking W.P., Steinsbu B.O., Steen I.H.;
RT "Complete Genome Sequence of the Thermophilic and Facultatively
RT Chemolithoautotrophic Sulfate Reducer Archaeoglobus sulfaticallidus Strain
RT PM70-1T.";
RL Genome Announc. 1:e00406-13(2013).
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; CP005290; AGK60377.1; -; Genomic_DNA.
DR RefSeq; WP_015589976.1; NC_021169.1.
DR AlphaFoldDB; N0BDR4; -.
DR STRING; 387631.Asulf_00348; -.
DR GeneID; 15391994; -.
DR KEGG; ast:Asulf_00348; -.
DR eggNOG; arCOG01179; Archaea.
DR HOGENOM; CLU_109098_1_2_2; -.
DR Proteomes; UP000013307; 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 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:UP000013307}.
FT DOMAIN 1..63
FT /note="S1-like"
FT /evidence="ECO:0000259|PROSITE:PS50832"
SQ SEQUENCE 78 AA; 9230 MW; 4CE2923B69BF5D1E CRC64;
MFAIVDSMLG AGHIKVRCED GEERLARIPG KMRKKIWIRE GDIVIIVPWP FQKSRADIVW
RYTIPQVEWL EKNGYLKF
//
