EF1D_SPUBR
ID EF1D_SPUBR Reviewed; 226 AA.
AC P93447;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Elongation factor 1-delta;
DE Short=EF-1-delta;
DE AltName: Full=Elongation factor 1B-beta;
DE AltName: Full=eEF-1B beta;
OS Spuriopimpinella brachycarpa (Chamnamul) (Pimpinella brachycarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Acronema clade;
OC Spuriopimpinella.
OX NCBI_TaxID=45043;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Shoot apex;
RA Moon Y.-H., Shin J.-S., Lim S.-H., Kim J.-C., Han T.-J., Cho S.H.,
RA Lee K.-W.;
RT "Nucleotide sequence of a cDNA clone for an elongation factor-1beta from
RT Pimpinella brachycarpa shoot-tip.";
RL (er) Plant Gene Register PGR97-057(1997).
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 (1B-alpha=beta'),
CC delta (1B-beta), and gamma (1B-gamma). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR EMBL; U87222; AAB68395.1; -; mRNA.
DR AlphaFoldDB; P93447; -.
DR SMR; P93447; -.
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; 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; PF00736; EF1_GNE; 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 2: Evidence at transcript level;
KW Elongation factor; Protein biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..226
FT /note="Elongation factor 1-delta"
FT /id="PRO_0000155039"
FT REGION 82..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..110
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 226 AA; 24497 MW; 3A22B60E4BFC7C75 CRC64;
MAVTFYDLSS EAGLEKLDEY LLSRSYISGY QASKDDLAVH AALAKPPSSK YVNVSRWYNH
VEALLRISGV SAEGCGVTVE GSSVATPPVA DTKASAAEDD DDDDVDLFGE ETEEEKKASE
ERAAAVKASG KKKESGKSSV LLDVKPWDDE TDMTKLEEAV RSIKMDGLLW GASKLVAVGY
GIKKLQIMLT IVDDLVSVDD LVEDYLTAEP ANEYIQSCDI VAFNKI