ID   IF2B_MALDO              Reviewed;         271 AA.
AC   P55871;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2001, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Eukaryotic translation initiation factor 2 subunit beta;
DE            Short=eIF-2-beta;
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Granny Smith;
RA   Dong Y.-H., Janssen B.-J., Bieleski L.L., Atkinson R.G., Morris B.A.,
RA   Gardner R.C.;
RT   "Isolating and characterizing genes differentially expressed early in apple
RT   fruit development.";
RL   J. Am. Soc. Hortic. Sci. 122:752-757(1997).
CC   -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis by
CC       forming a ternary complex with GTP and initiator tRNA. This complex
CC       binds to a 40S ribosomal subunit, followed by mRNA binding to form a
CC       43S preinitiation complex. Junction of the 60S ribosomal subunit to
CC       form the 80S initiation complex is preceded by hydrolysis of the GTP
CC       bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for
CC       eIF-2 to recycle and catalyze another round of initiation, the GDP
CC       bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by
CC       eIF-2B (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC   -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC06384.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U80269; AAC06384.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; P55871; -.
DR   SMR; P55871; -.
DR   STRING; 3750.XP_008363376.1; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR045196; IF2/IF5.
DR   InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR   InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR   InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR   PANTHER; PTHR23001; PTHR23001; 1.
DR   Pfam; PF01873; eIF-5_eIF-2B; 1.
DR   SMART; SM00653; eIF2B_5; 1.
DR   SUPFAM; SSF100966; SSF100966; 1.
DR   SUPFAM; SSF75689; SSF75689; 1.
PE   2: Evidence at transcript level;
KW   Initiation factor; Metal-binding; Protein biosynthesis; Zinc; Zinc-finger.
FT   CHAIN           1..271
FT                   /note="Eukaryotic translation initiation factor 2 subunit
FT                   beta"
FT                   /id="PRO_0000137412"
FT   ZN_FING         223..247
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   271 AA;  30343 MW;  516C98C17A52B477 CRC64;
     MADDNQNEVK DEVVADIAPF DPTKKKKKKE VVIQDTTDDS VGKLAEKAEA CTASEGQEST
     FAGLKKKKKK PIETSILNEE SGDAVEDLNE RTGEDEEGEG IVLETPSYPW EGSDRDYTYE
     ELLDRVFTIL RENNPDLAGD RRRTVMRPPQ VLREGTKKAV FVNFMDLCKT MHRQPDHVMA
     FLLAELGTSG SLDGQQRLVV KGRFAPKNFE GILRRYVNEY VICLGCQSPD TILSKENRLF
     FLRCEKCGSG RSVAPNKAGF MARVGRRNAG T