ID   EF1B2_CAEEL             Reviewed;         263 AA.
AC   Q9U2H9; A3RMU4; H9G359; H9G360;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Probable elongation factor 1-beta/1-delta 2;
DE            Short=EF-1-beta/delta 2;
GN   Name=eef-1B.2 {ECO:0000312|WormBase:Y41E3.10a};
GN   ORFNames=Y41E3.10 {ECO:0000312|WormBase:Y41E3.10a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000312|EMBL:CAB63360.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:CAB63360.2}
RP   PROTEIN SEQUENCE OF 2-11; 177-197; 201-222 AND 235-243, ACETYLATION AT
RP   SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA   Bienvenut W.V.;
RL   Submitted (APR-2006) to UniProtKB.
CC   -!- FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound
CC       to EF-1-alpha to GTP. {ECO:0000250|UniProtKB:P34460}.
CC   -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta, and gamma.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a {ECO:0000312|WormBase:Y41E3.10a};
CC         IsoId=Q9U2H9-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:Y41E3.10b};
CC         IsoId=Q9U2H9-2; Sequence=VSP_047489;
CC   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {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; Z95559; CAB63360.2; -; Genomic_DNA.
DR   EMBL; Z95559; CAM35842.1; -; Genomic_DNA.
DR   RefSeq; NP_001122811.1; NM_001129339.1. [Q9U2H9-2]
DR   RefSeq; NP_502816.2; NM_070415.5. [Q9U2H9-1]
DR   AlphaFoldDB; Q9U2H9; -.
DR   SMR; Q9U2H9; -.
DR   BioGRID; 43501; 39.
DR   STRING; 6239.Y41E3.10b; -.
DR   iPTMnet; Q9U2H9; -.
DR   World-2DPAGE; 0011:Q9U2H9; -.
DR   EPD; Q9U2H9; -.
DR   PaxDb; Q9U2H9; -.
DR   PeptideAtlas; Q9U2H9; -.
DR   EnsemblMetazoa; Y41E3.10a.1; Y41E3.10a.1; WBGene00012768. [Q9U2H9-1]
DR   EnsemblMetazoa; Y41E3.10b.1; Y41E3.10b.1; WBGene00012768. [Q9U2H9-2]
DR   GeneID; 178419; -.
DR   KEGG; cel:CELE_Y41E3.10; -.
DR   UCSC; Y41E3.10a.1; c. elegans.
DR   CTD; 178419; -.
DR   WormBase; Y41E3.10a; CE37568; WBGene00012768; eef-1B.2. [Q9U2H9-1]
DR   WormBase; Y41E3.10b; CE40788; WBGene00012768; eef-1B.2. [Q9U2H9-2]
DR   eggNOG; KOG1668; Eukaryota.
DR   eggNOG; KOG4174; Eukaryota.
DR   HOGENOM; CLU_050172_1_0_1; -.
DR   InParanoid; Q9U2H9; -.
DR   OMA; ETRYHEF; -.
DR   OrthoDB; 1464823at2759; -.
DR   PRO; PR:Q9U2H9; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00012768; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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; 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; SSF54984; SSF54984; 1.
DR   PROSITE; PS00824; EF1BD_1; 1.
DR   PROSITE; PS00825; EF1BD_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Direct protein sequencing;
KW   Elongation factor; Protein biosynthesis; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           2..263
FT                   /note="Probable elongation factor 1-beta/1-delta 2"
FT                   /id="PRO_0000155044"
FT   REGION          112..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|Ref.2"
FT   VAR_SEQ         115..263
FT                   /note="TSSVAAPAAAPAAAKEEAAGDDDFDLFGSEDEEEDEEKKKVVEERLAAYAAK
FT                   KATKAGPIAKSSVILDVKPWDDETDLGEMEKLVRSIEMDGLVWGGAKLIPIGYGIKKLQ
FT                   IITVIEDLKVSVDDLIEKITGDFEDHVQSVDIVAFNKI -> VNHRRHVLILGDGNLSF
FT                   SLAIASSDPETVYFATVFDSKEQFLKKYNAHDTLNALDALSNVILCFGVDATDLPVRWS
FT                   NIFNTVIMNFPHPGGKTNLRKSKILLSGIFASLRSIMDSQAVFLLSLAIGQSGLEKVSD
FT                   PWMNELPSHKKDSWQAIYLGAENGFILDSLERFDTDRFASYRSSGYKETKKGFNNREGL
FT                   TFSFKKCDNQQKSLRDFQLAEPPRSGKFKFNYYRPFYAQDLSILFKIGESEGEKLAVEL
FT                   VKSIAGNCLAAISEIEYLRSICPDPPLPNRIYRIIWHGLELPMGREMCSRIHEELRNRI
FT                   AEEIVANNLPLVLT (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_047489"
SQ   SEQUENCE   263 AA;  28173 MW;  C1DC39F5A73EDB91 CRC64;
     MSVEGLLSEV KHFNAHHLDA ALGEQLFYGG KRVFSDVKPG TSSGGDHGCK GGKSELKGAI
     HNAKHAADKA LNKEGGEDVS KLREEHSALA KKVDDLASLV AELQLQLSTL RQGQTSSVAA
     PAAAPAAAKE EAAGDDDFDL FGSEDEEEDE EKKKVVEERL AAYAAKKATK AGPIAKSSVI
     LDVKPWDDET DLGEMEKLVR SIEMDGLVWG GAKLIPIGYG IKKLQIITVI EDLKVSVDDL
     IEKITGDFED HVQSVDIVAF NKI