EF1B_ARTSA
ID EF1B_ARTSA Reviewed; 207 AA.
AC P12262;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Elongation factor 1-beta;
DE Short=EF-1-beta;
OS Artemia salina (Brine shrimp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Anostraca; Artemiidae; Artemia.
OX NCBI_TaxID=85549;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT ALA-2, AND PARTIAL PROTEIN SEQUENCE.
RA Maessen G.D.F., Amons R., Maassen J.A., Moeller W.;
RT "Primary structure of elongation factor 1-beta from Artemia.";
RL FEBS Lett. 208:77-83(1986).
RN [2]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=2207149; DOI=10.1016/0167-4781(90)90174-z;
RA van Damme H.T.F., Amons R., Karssies R., Timmers C.J., Janssen G.M.C.,
RA Moeller W.;
RT "Elongation factor 1 beta of artemia: localization of functional sites and
RT homology to elongation factor 1 delta.";
RL Biochim. Biophys. Acta 1050:241-247(1990).
RN [3]
RP PHOSPHORYLATION AT SER-90.
RX PubMed=3403515; DOI=10.1016/s0021-9258(18)37920-1;
RA Janssen G.M.C., Maessen G.D.F., Amons R., Moeller W.;
RT "Phosphorylation of elongation factor 1 beta by an endogenous kinase
RT affects its catalytic nucleotide exchange activity.";
RL J. Biol. Chem. 263:11063-11066(1988).
CC -!- FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound
CC to EF-1-alpha to GTP.
CC -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta, and gamma.
CC -!- PTM: Phosphorylation affects the GDP/GTP exchange rate.
CC {ECO:0000269|PubMed:3403515}.
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR EMBL; M35636; AAC83402.1; -; mRNA.
DR AlphaFoldDB; P12262; -.
DR SMR; P12262; -.
DR iPTMnet; P12262; -.
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 Acetylation; Direct protein sequencing; Elongation factor; Phosphoprotein;
KW Protein biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.1"
FT CHAIN 2..207
FT /note="Elongation factor 1-beta"
FT /id="PRO_0000155028"
FT REGION 70..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.1"
FT MOD_RES 90
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:3403515"
SQ SEQUENCE 207 AA; 23324 MW; ED7A7C9FDB8F75E5 CRC64;
MANIDLKAEK GQEQLNELLA NKSYLQGYEP SQEDVAAFNQ LNKAPSDKFP YLLRWYKHIS
SFSDAEKKGF PGIPTSASKE EDDDVDLFGS DEEDEEAEKI KAERMKAYSD KKSKKPAIVA
KSSVILDIKP WDDETDMAEM EKLVRSVQMD GLVWGAAKLI PLAYGIKKLS IMCVVEDDKV
SIDELQEKIS EFEDFVQSVD IAAFNKV
