ID G8JV46_ERECY Unreviewed; 638 AA.
AC G8JV46;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
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 OrderedLocusNames=Ecym_6134 {ECO:0000313|EMBL:AET40525.1};
OS Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 /
OS NRRL Y-17582) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=931890 {ECO:0000313|EMBL:AET40525.1, ECO:0000313|Proteomes:UP000006790};
RN [1] {ECO:0000313|Proteomes:UP000006790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582
RC {ECO:0000313|Proteomes:UP000006790};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
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}.
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DR EMBL; CP002502; AET40525.1; -; Genomic_DNA.
DR RefSeq; XP_003647342.1; XM_003647294.1.
DR AlphaFoldDB; G8JV46; -.
DR STRING; 931890.G8JV46; -.
DR GeneID; 11468893; -.
DR KEGG; erc:Ecym_6134; -.
DR eggNOG; KOG2315; Eukaryota.
DR HOGENOM; CLU_013809_0_1_1; -.
DR InParanoid; G8JV46; -.
DR OMA; WNPNSKE; -.
DR OrthoDB; 22264at2759; -.
DR Proteomes; UP000006790; Chromosome 6.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
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 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:UP000006790};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845,
KW ECO:0000256|PIRNR:PIRNR017222}.
FT DOMAIN 218..416
FT /note="Translation initiation factor beta propellor-like"
FT /evidence="ECO:0000259|Pfam:PF08662"
FT REGION 466..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 638 AA; 71090 MW; 85FA5456682AB7F5 CRC64;
MSFQLFAKTP VESEIFEGYP SFRKLDLCES PNFITSKLSP CGRFIAISTE SRVQVFKNGD
FQDVLLELKL KDVYDLEFSP GGSYLSTWER PHIDNETHEN VKIWYLNEEE PSAEEVKYQY
QARTQNAWAL QFSKLDNYAV RRFGKELRIS KLDHAAPKFN FDRPYAKLVP DGQVSRYLIS
PAEHPTICTF SPEKGGKPAQ LTIYPITEGT IQKKIVSKIF FKADSCQLKW NALGNAVLCL
AITDFDASNQ SYYGENTLYL LSFQGVNGSL GGESVRVPLG KEGPIHDFTW SPTSRQFGVI
YGFMPATITF FDIRGNAVHS LTEQRKNTMI YSPSGRYILI AGFGNLQGAV EILDRHDKFK
CITKFDAANT STCTWSPGGE FILTATTSPR LRVDNGLKVW HVSGKLCFVN EYAGLLEASW
RYPCIYKVKQ PGSHVIVNWD SKKLQDSPAL KDPVLNPSQV EIHPSVTAYN EKNPKKNNGT
SSVSKPVGAY KPPHARRAAA TGSSVPGAAV KPAVPGMTPK ASKGLVPGMA PKESKSQAKN
RKKREHGHSR KAAPTNADSD DNPSSIATTP EPKEMPKPNK ETSPEEKKIR SLLKKLRAIE
SLKQRQAVGD KLEDTQILKI QSEQKVLQEL NLLSFSEP
//
