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Database: UniProt
Entry: A0A397V2S8_9GLOM
LinkDB: A0A397V2S8_9GLOM
Original site: A0A397V2S8_9GLOM 
ID   A0A397V2S8_9GLOM        Unreviewed;        61 AA.
AC   A0A397V2S8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=S1-like domain-containing protein {ECO:0000259|PROSITE:PS50832};
DE   Flags: Fragment;
GN   ORFNames=C2G38_2317178 {ECO:0000313|EMBL:RIB16221.1};
OS   Gigaspora rosea.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Diversisporales; Gigasporaceae; Gigaspora.
OX   NCBI_TaxID=44941 {ECO:0000313|EMBL:RIB16221.1, ECO:0000313|Proteomes:UP000266673};
RN   [1] {ECO:0000313|EMBL:RIB16221.1, ECO:0000313|Proteomes:UP000266673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM 194757 {ECO:0000313|EMBL:RIB16221.1,
RC   ECO:0000313|Proteomes:UP000266673};
RA   Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA   Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA   Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT   "Comparative genomics reveals the genomic features of Rhizophagus
RT   irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT   symbiotic lifestyle signature.";
RL   Submitted (JUN-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}.
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:RIB16221.1}.
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DR   EMBL; QKWP01000692; RIB16221.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397V2S8; -.
DR   STRING; 44941.A0A397V2S8; -.
DR   Proteomes; UP000266673; 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   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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   4: Predicted;
KW   Initiation factor {ECO:0000256|PROSITE-ProRule:PRU00181};
KW   Protein biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00181};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266673}.
FT   DOMAIN          6..61
FT                   /note="S1-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50832"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RIB16221.1"
SQ   SEQUENCE   61 AA;  7226 MW;  B69C735F5F8798C0 CRC64;
     FLLIKYAQVV KMLENDRLEA QCFDGEKRLA RIHSKLQKKL NNCDIILISF HDYQDAKAEL
     F
//
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