ID A0A1I7SDF1_BURXY Unreviewed; 558 AA.
AC A0A1I7SDF1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Eukaryotic translation initiation factor 2A {ECO:0000256|ARBA:ARBA00013819};
GN ORFNames=BXYJ_LOCUS14802 {ECO:0000313|EMBL:CAD5234711.1};
OS Bursaphelenchus xylophilus (Pinewood nematode worm) (Aphelenchoides
OS xylophilus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Aphelenchoidea; Aphelenchoididae;
OC Bursaphelenchus.
OX NCBI_TaxID=6326 {ECO:0000313|Proteomes:UP000095284, ECO:0000313|WBParaSite:BXY_1105600.1};
RN [1] {ECO:0000313|WBParaSite:BXY_1105600.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:CAG9130649.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ka4C1 {ECO:0000313|EMBL:CAD5234711.1};
RA Kikuchi T.;
RL Submitted (AUG-2020) 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 -!- SIMILARITY: Belongs to the WD repeat EIF2A family.
CC {ECO:0000256|ARBA:ARBA00009573}.
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DR EMBL; CAJFDI010000006; CAD5234711.1; -; Genomic_DNA.
DR EMBL; CAJFCV020000006; CAG9130649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7SDF1; -.
DR WBParaSite; BXY_1105600.1; BXY_1105600.1; BXY_1105600.
DR eggNOG; KOG2315; Eukaryota.
DR Proteomes; UP000095284; Unplaced.
DR Proteomes; UP000582659; Unassembled WGS sequence.
DR Proteomes; UP000659654; Unassembled WGS sequence.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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 InterPro; IPR036322; WD40_repeat_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 SUPFAM; SSF50978; WD40 repeat-like; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000659654};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT DOMAIN 222..407
FT /note="Translation initiation factor beta propellor-like"
FT /evidence="ECO:0000259|Pfam:PF08662"
FT REGION 479..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 502..556
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 487..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 558 AA; 63325 MW; C0C8E7CBA95CAD0E CRC64;
MAEKLVYAYR SANGLKIRRG LENAEDILSL NCSSKDDAVC RCFQFSPSGR FFAYCDNKRT
VCYDVVSKKE RFAIEGLGRT MKLTFSPNEN LLITYQQYAI YGMRTGEDGV KREPEPNLRF
YDIRDGKEVA AKICKSQANW KPQFSTDEKF CVLKENGSEL HFYENNKFDR FTRKGVIKGL
ETFELGPGLD PSLCCFIPSV GGKPGLIQLR NPHDELRVIT QKTSFNCDVC SFNWNSKGSA
VLATTTVEVD KTNQSYYGIS CLYLLTKMGD SFQVHLNKEG PLHSLEWSPN GMSFIACFGY
MPAKICVFNL RATSIWCLGE SHKNEVYYNP FGSLLAVCGF GNLAAGKIEV WDVEKKTEVV
QMEVPNTTYF SWAPDGQHFM TATTSPRLRV DNNFRIWHYT GQLKYEYLSV DSEKKAVEMA
QVVFKPAPGI FNKFKIIELT DAERRKIENR RVTSSIPDHS VTFLKNAGVV SEGGRYVPPH
LRKSIDPSPR ANQNSSGPRV ELTANEKQIQ KLKKKIEDIK KLKQKTADGI KLELNQRQKL
DKLPELEAEL KQLEMNGS
//
