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Database: UniProt
Entry: A0A0V1MD85_9BILA
LinkDB: A0A0V1MD85_9BILA
Original site: A0A0V1MD85_9BILA 
ID   A0A0V1MD85_9BILA        Unreviewed;       397 AA.
AC   A0A0V1MD85;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Eukaryotic translation initiation factor 2A {ECO:0000256|ARBA:ARBA00013819};
GN   Name=EIF2A {ECO:0000313|EMBL:KRZ69751.1};
GN   ORFNames=T10_9276 {ECO:0000313|EMBL:KRZ69751.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ69751.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ69751.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ69751.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-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   -!- SIMILARITY: Belongs to the WD repeat EIF2A family.
CC       {ECO:0000256|ARBA:ARBA00009573}.
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:KRZ69751.1}.
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DR   EMBL; JYDO01000129; KRZ69751.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1MD85; -.
DR   Proteomes; UP000054843; 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; 1.
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   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW   ECO:0000313|EMBL:KRZ69751.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT   DOMAIN          274..385
FT                   /note="Translation initiation factor beta propellor-like"
FT                   /evidence="ECO:0000259|Pfam:PF08662"
FT   REGION          31..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   397 AA;  45083 MW;  0ACA091AE81B0E99 CRC64;
     MRPLTERAQF TNVMGFRTVF AVVEGEQERR VLQRRQDKPR SDKRLTDSKP MSTDAEKAEL
     GHLPKFALRD DGNITVYAGI KNPVQVFTHE CRACISGATL TFSNDGKYFA FCDEKIYVFK
     CSKWKLHAAF DENEATNLFF SPKTSVLCTF KPYSTAVGVT SVESNLKLWS MVTGKLLCEW
     VQKNIVSWRP MWTADESIVA RLVGSELWFS APENLNRYIQ KLTLPKLSSF SLSPGPAPFH
     VAVYTASSRE KMASARLYSC SLNWPIDIIA CKNFQADRVD FHWNKNGTAV LVMAILDVDP
     QNKSYYGCEN LHLMTTCGVA CNVPLDREGP IHSVDWHPGS KLFCVVYGYI PSKAALFDLK
     ANRVFDFGCE PRNEVHFNRF GNYILSWNNF IIFFSLS
//
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