ID A0A4E0Q7A9_9EURY Unreviewed; 105 AA.
AC A0A4E0Q7A9;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 18-JUN-2025, entry version 20.
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:TGC06771.1};
GN Synonyms=eif1a {ECO:0000256|HAMAP-Rule:MF_00216};
GN ORFNames=CUN85_12475 {ECO:0000313|EMBL:TGC06771.1};
OS Methanolobus halotolerans.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanolobus.
OX NCBI_TaxID=2052935 {ECO:0000313|EMBL:TGC06771.1, ECO:0000313|Proteomes:UP000297295};
RN [1] {ECO:0000313|EMBL:TGC06771.1, ECO:0000313|Proteomes:UP000297295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY-01 {ECO:0000313|EMBL:TGC06771.1,
RC ECO:0000313|Proteomes:UP000297295};
RA Shen Y., Huang H.-H., Lai M.-C., Chen S.-C.;
RT "Isolation and Characterization of Methanogenic Archaea from Saline
RT Meromictic Lake at Siberia.";
RL Submitted (NOV-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TGC06771.1}.
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DR EMBL; PGGK01000022; TGC06771.1; -; Genomic_DNA.
DR RefSeq; WP_135390623.1; NZ_PGGK01000022.1.
DR AlphaFoldDB; A0A4E0Q7A9; -.
DR OrthoDB; 2586at2157; -.
DR Proteomes; UP000297295; Unassembled WGS sequence.
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 NCBIfam; NF003084; PRK04012.1-3; 1.
DR NCBIfam; NF003085; PRK04012.1-5; 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|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00216};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00216, ECO:0000256|PROSITE-
KW ProRule:PRU00181}; Reference proteome {ECO:0000313|Proteomes:UP000297295}.
FT DOMAIN 16..90
FT /note="S1-like"
FT /evidence="ECO:0000259|PROSITE:PS50832"
SQ SEQUENCE 105 AA; 12207 MW; 06465458C1D25721 CRC64;
MQKRKHVDNA DLTAVTRVRT PSKENKEVLA IVESMLGANH VRLRCMDGVL RMGRIPGSMK
KKTWIREGDI VIAVPWEFQN EKADVIWKYT RLQVSWLERK GYLKG
//
