ID A0A2I8VNU1_9EURY Unreviewed; 96 AA.
AC A0A2I8VNU1;
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:AUV83565.1};
GN Synonyms=eif1a {ECO:0000256|HAMAP-Rule:MF_00216};
GN ORFNames=C2R22_19545 {ECO:0000313|EMBL:AUV83565.1};
OS Salinigranum rubrum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Salinigranum.
OX NCBI_TaxID=755307 {ECO:0000313|EMBL:AUV83565.1, ECO:0000313|Proteomes:UP000236584};
RN [1] {ECO:0000313|EMBL:AUV83565.1, ECO:0000313|Proteomes:UP000236584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GX10 {ECO:0000313|EMBL:AUV83565.1,
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}.
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; CP026309; AUV83565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I8VNU1; -.
DR KEGG; srub:C2R22_19545; -.
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 8..82
FT /note="S1-like"
FT /evidence="ECO:0000259|PROSITE:PS50832"
SQ SEQUENCE 96 AA; 11359 MW; E53D7E65EABD4614 CRC64;
MAKDGDETRR DLRMPDDDEV FAVVTEMLGA NRVKVRCADG VERTARIPGR MQKRIWIRED
DVVLVEPWDW QDEKADISWR YEKSEADQLR EEGHIQ
//