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Database: UniProt
Entry: S7WAD9_SPRLO
LinkDB: S7WAD9_SPRLO
Original site: S7WAD9_SPRLO 
ID   S7WAD9_SPRLO            Unreviewed;       118 AA.
AC   S7WAD9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Eukaryotic translation initiation factor 1A {ECO:0000313|EMBL:EPR79851.1};
GN   ORFNames=SLOPH_345 {ECO:0000313|EMBL:EPR79851.1};
OS   Spraguea lophii (strain 42_110) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Spraguidae;
OC   Spraguea.
OX   NCBI_TaxID=1358809 {ECO:0000313|EMBL:EPR79851.1, ECO:0000313|Proteomes:UP000014978};
RN   [1] {ECO:0000313|Proteomes:UP000014978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=42_110 {ECO:0000313|Proteomes:UP000014978};
RX   PubMed=23990793; DOI=10.1371/journal.pgen.1003676;
RA   Campbell S.E., Williams T.A., Yousuf A., Soanes D.M., Paszkiewicz K.H.,
RA   Williams B.A.P.;
RT   "The genome of Spraguea lophii and the basis of host-microsporidian
RT   interactions.";
RL   PLoS Genet. 9:E1003676-E1003676(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}.
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:EPR79851.1}.
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DR   EMBL; ATCN01000088; EPR79851.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7WAD9; -.
DR   STRING; 1358809.S7WAD9; -.
DR   VEuPathDB; MicrosporidiaDB:SLOPH_345; -.
DR   HOGENOM; CLU_109098_1_1_1; -.
DR   InParanoid; S7WAD9; -.
DR   OMA; RKKVWMS; -.
DR   OrthoDB; 2919581at2759; -.
DR   Proteomes; UP000014978; 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   PANTHER; PTHR21668; EIF-1A; 1.
DR   PANTHER; PTHR21668:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 4C; 1.
DR   Pfam; PF01176; eIF-1a; 1.
DR   SMART; SM00652; eIF1a; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50832; S1_IF1_TYPE; 1.
PE   3: Inferred from homology;
KW   Initiation factor {ECO:0000256|PROSITE-ProRule:PRU00181,
KW   ECO:0000313|EMBL:EPR79851.1};
KW   Protein biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00181};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014978}.
FT   DOMAIN          20..87
FT                   /note="S1-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50832"
SQ   SEQUENCE   118 AA;  13717 MW;  96AD4EC21B94CCCB CRC64;
     MAKNKSKRKQ NVPTTLEYSE EGVSIYGQVL KPLGSCRFKV SCSDSIIRVC KARGSFHRRV
     WINESDIVLL VFREGEPNKG DIVRKYLPYE VKVLRDSKEI PENFNREETV TNFEFETI
//
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