ID   A0A0N0BI31_9HYME        Unreviewed;       518 AA.
AC   A0A0N0BI31;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Eukaryotic translation initiation factor 2A {ECO:0000313|EMBL:KOX77092.1};
GN   ORFNames=WN51_10486 {ECO:0000313|EMBL:KOX77092.1};
OS   Melipona quadrifasciata.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Melipona.
OX   NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX77092.1, ECO:0000313|Proteomes:UP000053105};
RN   [1] {ECO:0000313|EMBL:KOX77092.1, ECO:0000313|Proteomes:UP000053105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0111107301 {ECO:0000313|EMBL:KOX77092.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KOX77092.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Melipona quadrifasciata.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions in the early steps of protein synthesis of a small
CC       number of specific mRNAs. Acts by directing the binding of methionyl-
CC       tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it
CC       binds methionyl-tRNAi to 40S subunits in a codon-dependent manner,
CC       whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a
CC       GTP-dependent manner. {ECO:0000256|ARBA:ARBA00003993}.
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; KQ435736; KOX77092.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0BI31; -.
DR   STRING; 166423.A0A0N0BI31; -.
DR   OrthoDB; 22264at2759; -.
DR   Proteomes; UP000053105; Unassembled WGS sequence.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011387; TIF2A.
DR   InterPro; IPR013979; TIF_beta_prop-like.
DR   PANTHER; PTHR13227; EUKARYOTIC TRANSLATION INITIATION FACTOR 2A; 1.
DR   PANTHER; PTHR13227:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 2A; 1.
DR   Pfam; PF08662; eIF2A; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE   4: Predicted;
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW   ECO:0000313|EMBL:KOX77092.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT   DOMAIN          208..297
FT                   /note="Translation initiation factor beta propellor-like"
FT                   /evidence="ECO:0000259|Pfam:PF08662"
FT   REGION          416..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   518 AA;  58858 MW;  E217C3A9C5444C6B CRC64;
     MALTVPCVAV RGSIGISLGQ GPPSYEPVKS FPKDDSKTCK AMVFSPEGRY FAWVNGMTAN
     ILHCSTWKII IEIKRPKISA IQFSTRSTYF MTWEPFIGTP NLHIWKSETG ELVKSFIQKK
     QSDWEPQWTS DEKICGILVG ADVILYEDVN FNKIMYRINV AKVARFSISP SNTPYYILCY
     MPGKSDQPSF ARLFQYPKFE FTQALANKSF FQADRVNVYW NNNGTSVLLM TSTEVDKTGA
     SYYGKQTLHY LSTKGETSMV MLSNKGPIHA VQWSPKNNEF CVIYDFMPAK ATLFNLKKLI
     AKTEAPDTTL LQWSPDGEHF MTATTAPRLR MGNGFKIWHY TGTLLYERPW NEQEELWEVL
     WQTFPPETFP EKPISYKAVE GIAPSQPQAS KQVYRPPSAR GETICFKLRD DELHKAGIKK
     NPKSKKKTKK GTSESSQSSN PSTNGQVTTS TETQNLTTNV PECDNLERSK KIKKIKSKLE
     QISKLKELQV AGKQLEINQL DKIKKEADLM KELEELAL
//