ID   A0A1Y2EBH1_9PEZI        Unreviewed;       698 AA.
AC   A0A1Y2EBH1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   28-JUN-2023, entry version 19.
DE   RecName: Full=Eukaryotic translation initiation factor 2A {ECO:0000256|ARBA:ARBA00013819, ECO:0000256|PIRNR:PIRNR017222};
DE            Short=eIF-2A {ECO:0000256|PIRNR:PIRNR017222};
GN   ORFNames=BCR38DRAFT_406137 {ECO:0000313|EMBL:ORY68185.1};
OS   Pseudomassariella vexata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX   NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY68185.1, ECO:0000313|Proteomes:UP000193689};
RN   [1] {ECO:0000313|EMBL:ORY68185.1, ECO:0000313|Proteomes:UP000193689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY68185.1,
RC   ECO:0000313|Proteomes:UP000193689};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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|PIRNR:PIRNR017222}.
CC   -!- SIMILARITY: Belongs to the WD repeat EIF2A family.
CC       {ECO:0000256|ARBA:ARBA00009573, ECO:0000256|PIRNR:PIRNR017222}.
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:ORY68185.1}.
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DR   EMBL; MCFJ01000003; ORY68185.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2EBH1; -.
DR   STRING; 1141098.A0A1Y2EBH1; -.
DR   InParanoid; A0A1Y2EBH1; -.
DR   OrthoDB; 22264at2759; -.
DR   Proteomes; UP000193689; Unassembled WGS sequence.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR011387; TIF2A.
DR   InterPro; IPR013979; TIF_beta_prop-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
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   PIRSF; PIRSF017222; eIF2A; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW   ECO:0000256|PIRNR:PIRNR017222};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|PIRNR:PIRNR017222};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193689};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845,
KW   ECO:0000256|PIRNR:PIRNR017222}.
FT   DOMAIN          216..410
FT                   /note="Translation initiation factor beta propellor-like"
FT                   /evidence="ECO:0000259|Pfam:PF08662"
FT   REGION          470..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          678..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..574
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..603
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..618
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   698 AA;  76264 MW;  A1807BA6F977B124 CRC64;
     MANPLQFAYR TQKAIGITDA APVYHPVPGF VQPEGNLRCC VYSQCGRYLA WATNDRVTIV
     DASTGHVLTS VSVVNVFEVA FSPRGSFFST WERPAKDEAG DATKNLKVWR TIEDAPQDTE
     KQPLGRFVQK SQSGWNLQYT TDEKFCARMV TNEVQFYDSN DLSTVWNKLR IEGVADFAIT
     PGQSYNVAVF VPERKGQPAA VKVFNVPQFT SPISQKTFFK GDKVQLKWNS LGTSLIVLAQ
     TDVDKSNKSY YGETTLYLLS VNGAFDARVS LDKEGPIHDV TWSPNGKEFG VIYGFMPAKT
     TIFNHRAVAT HSFALGPRNT IIFSPTGRFV LVAGFGNLAG QIDVYDLEKD YRKVCTIESG
     SPSVCLWSPD SRYIMTATTS PRLRVDNGVK LWHVGGTIIY NEDMVELYNV IWRPAPLETL
     PKEDPLQPVP TPHSSAVAYL GTVKTPSKPV GAYRPPGARG MATPLSFRRE DEGGSAHVMS
     NGAANIGPNG FGRSRRQVPG AELTESAPRG IPGAEPVPSV PGVDGDEALS KAALKNKKKR
     SNKKNKGPDG GNPTNGGLAP PGQEQGTGNS HVGRSPERRG QHSNQQHRSR SRNPMGNRNR
     SNTARNGDGH HHRDGGASLH PLPHGQTAQH STPETPLSPG NQNPAAKKLR ALQKKVRAIE
     DLEMRLAGGE KLEDTQMKKI STKSSVQKEL DALEKESR
//