ID   EF1B2_BOMMO             Reviewed;         222 AA.
AC   P29522;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Elongation factor 1-beta';
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-34.
RX   PubMed=1480492; DOI=10.1093/nar/20.24.6734;
RA   Taira H., Kamiie K., Kakuta A., Ooura H., Matsumoto S., Ejiri S.,
RA   Katsumata T.;
RT   "Nucleotide sequence of the cDNA encoding silk gland elongation factor 1
RT   beta'.";
RL   Nucleic Acids Res. 20:6734-6734(1992).
CC   -!- FUNCTION: EF-1-beta and EF-1-beta' stimulate the exchange of GDP bound
CC       to EF-1-alpha to GTP.
CC   -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, beta' and gamma.
CC   -!- PTM: Phosphorylated.
CC   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR   EMBL; D13339; BAA02602.1; -; mRNA.
DR   PIR; S35514; S35514.
DR   RefSeq; NP_001037556.1; NM_001044091.1.
DR   AlphaFoldDB; P29522; -.
DR   SMR; P29522; -.
DR   STRING; 7091.BGIBMGA008921-TA; -.
DR   GeneID; 693119; -.
DR   KEGG; bmor:693119; -.
DR   CTD; 693119; -.
DR   eggNOG; KOG1668; Eukaryota.
DR   HOGENOM; CLU_050172_0_2_1; -.
DR   OrthoDB; 1464823at2759; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd00292; EF1B; 1.
DR   Gene3D; 3.30.70.60; -; 1.
DR   InterPro; IPR036219; eEF-1beta-like_sf.
DR   InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR   InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR   InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR   Pfam; PF10587; EF-1_beta_acid; 1.
DR   Pfam; PF00736; EF1_GNE; 1.
DR   SMART; SM01182; EF-1_beta_acid; 1.
DR   SMART; SM00888; EF1_GNE; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF54984; SSF54984; 1.
DR   PROSITE; PS00824; EF1BD_1; 1.
DR   PROSITE; PS00825; EF1BD_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Elongation factor; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1480492"
FT   CHAIN           2..222
FT                   /note="Elongation factor 1-beta'"
FT                   /id="PRO_0000155029"
FT   REGION          71..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..112
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   222 AA;  24549 MW;  54BD68A4C004271A CRC64;
     MAVGDVKTAQ GLNDLNQYLA EKSYVSGYTP SQADVQVFEQ VGKAPAANLP HVLRWYNQIA
     SYTSAERKTW SQGTSPLTAG AKPTAPAPAA KDDDDDDVDL FGSGDEEEDA EAERIREERL
     KAYADKKSKK PALIAKSSIL LDVKPWDDET DMKEMENQVR TIEMEGLLWG ASKLVPVGYG
     INKLQIMCVI EDDKVSVDLL TEKIQEFEDF VQSVDIAAFN KI