IF2B_WHEAT
ID IF2B_WHEAT Reviewed; 270 AA.
AC O24473;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit beta;
DE Short=eIF-2-beta;
DE AltName: Full=P38;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=9185629; DOI=10.1006/abbi.1997.0119;
RA Metz A.M., Browning K.S.;
RT "Assignment of the beta-subunit of wheat eIF2 by protein and DNA sequence
RT analysis and immunoanalysis.";
RL Arch. Biochem. Biophys. 342:187-189(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}.
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DR EMBL; U87163; AAB65774.1; -; mRNA.
DR PIR; T06992; T06992.
DR AlphaFoldDB; O24473; -.
DR SMR; O24473; -.
DR STRING; 4565.Traes_4BL_BB500A981.1; -.
DR PRIDE; O24473; -.
DR eggNOG; KOG2768; Eukaryota.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; O24473; baseline and differential.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
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 1: Evidence at protein level;
KW Direct protein sequencing; Initiation factor; Metal-binding;
KW Protein biosynthesis; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..270
FT /note="Eukaryotic translation initiation factor 2 subunit
FT beta"
FT /id="PRO_0000137413"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 6..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 270 AA; 30389 MW; D1AED918C2F36455 CRC64;
MADEEQMERK EEATEIAPFD PTKKKKKKKV VIQDPADEVD KLAEKTEGLS VTESGEASFV
GLKKKKKKLV ELDPSLVEAG DGEDTLDDQV GEDEQGEGIV LGGATQYPWE GTDRDYKYDE
LLGRVFNILR ENNPDLAGDR RRTVMRPPQV LREGTKKTVF VNFMDLCKTM HRQPEHVMMF
LLAEMGTSGS LDGQQRLVIK GRFAPKNFEA ILRRYINEYV ICHGCKSPDT ILSKENRLFF
LRCEQCGSSR SVAPIKAGFV AQVGRRKAGT
