ID   EIF2A_DICDI             Reviewed;         608 AA.
AC   Q54PV7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Eukaryotic translation initiation factor 2A;
DE            Short=eIF-2A;
GN   Name=eif2a; ORFNames=DDB_G0284267;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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:0000250|UniProtKB:Q9BY44}.
CC   -!- SIMILARITY: Belongs to the WD repeat EIF2A family. {ECO:0000305}.
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DR   EMBL; AAFI02000064; EAL65322.1; -; Genomic_DNA.
DR   RefSeq; XP_638688.1; XM_633596.1.
DR   AlphaFoldDB; Q54PV7; -.
DR   SMR; Q54PV7; -.
DR   STRING; 44689.DDB0234177; -.
DR   PaxDb; Q54PV7; -.
DR   EnsemblProtists; EAL65322; EAL65322; DDB_G0284267.
DR   GeneID; 8624518; -.
DR   KEGG; ddi:DDB_G0284267; -.
DR   dictyBase; DDB_G0284267; eIF2a.
DR   eggNOG; KOG2315; Eukaryota.
DR   HOGENOM; CLU_013809_1_0_1; -.
DR   InParanoid; Q54PV7; -.
DR   OMA; LITWQRP; -.
DR   PhylomeDB; Q54PV7; -.
DR   PRO; PR:Q54PV7; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; ISS:dictyBase.
DR   GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR   GO; GO:0006413; P:translational initiation; ISS:dictyBase.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR011387; TIF2A.
DR   InterPro; IPR013979; TIF_beta_prop-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR13227; PTHR13227; 1.
DR   Pfam; PF08662; eIF2A; 1.
DR   PIRSF; PIRSF017222; eIF2A; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Initiation factor; Protein biosynthesis; Reference proteome;
KW   Repeat; Translation regulation; WD repeat.
FT   CHAIN           1..608
FT                   /note="Eukaryotic translation initiation factor 2A"
FT                   /id="PRO_0000331243"
FT   REPEAT          115..161
FT                   /note="WD 1"
FT   REPEAT          207..255
FT                   /note="WD 2"
FT   REPEAT          310..350
FT                   /note="WD 3"
FT   REPEAT          351..393
FT                   /note="WD 4"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          550..608
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        466..485
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..544
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   608 AA;  68034 MW;  129DD3E6E77BDF79 CRC64;
     MSAPNNNNNN TTTTTTTSPS PSQSSPTLTS VASNSTTTTT TETLTTPKLQ FVVRSKTNAY
     QEIGQQYGKN LNLPSYSNGD CRHVEYSKDG TLIAYVNLNE IVICNSDGGS VHSVINRPNV
     GMISFSPQNS FLLTWERMSE YNNNENNLIV WDIKQASILY KTSQKYCNQE NWPLIKWTDD
     EVLAGKLISN EVHFFNGRSI GVLAKKIKLQ DISSFEFAPA TNGGPYKIAT FVPEKGSTPG
     SARIYSYPTV NEYCSHLKFF KASEAKVLWN KKGNAILVHT FTDTDKSGKS YYGETGLWFL
     SQDGSSFNLN IKGPIHDVQW SPTLDQFMVC YGNMPSQTTL FNLKGEPLVD FGLNPRNTIR
     FSPNGQLLCL GGFGNLQGDM DFWDLTRYKR ICGTQSHCAI YTEWSADSVH FMTAVLSPRI
     RVDNGVKIIK YDNTIVYQEN IPELYQASWR PLNPLVFPNE RIVYPSIQQQ KESSPQPQKY
     TPPSLRNMQA APPVVTSPPA MGAPLPSGFK VYLASAKSSS TFKPKQKPSS TTTTNNTTTT
     TTKPAADEPK RELTPIEKKI RNVERKLKEV EVLKEKLNSG EFIPPTAIEK INNEQKFLEE
     LRKLQSEL