ID A0A3Q3L6X4_9TELE Unreviewed; 229 AA.
AC A0A3Q3L6X4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Elongation factor 1-beta {ECO:0000256|ARBA:ARBA00017600};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000005374.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000005374.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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:0000256|ARBA:ARBA00002937}.
CC -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta, and gamma.
CC {ECO:0000256|ARBA:ARBA00011613}.
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
CC {ECO:0000256|ARBA:ARBA00007411, ECO:0000256|RuleBase:RU003791}.
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DR AlphaFoldDB; A0A3Q3L6X4; -.
DR STRING; 205130.ENSMAMP00000005374; -.
DR Ensembl; ENSMAMT00000005516.2; ENSMAMP00000005374.1; ENSMAMG00000002893.2.
DR GeneTree; ENSGT00950000183014; -.
DR InParanoid; A0A3Q3L6X4; -.
DR OrthoDB; 77945at2759; -.
DR Proteomes; UP000261640; Unplaced.
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 CDD; cd10308; GST_C_eEF1b_like; 1.
DR Gene3D; 1.20.1050.130; -; 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; IPR049720; EF1B_bsu/dsu.
DR InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR014717; Transl_elong_EF1B/ribsomal_bS6.
DR InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR PANTHER; PTHR11595; EF-HAND AND COILED-COIL DOMAIN-CONTAINING FAMILY MEMBER; 1.
DR PANTHER; PTHR11595:SF21; ELONGATION FACTOR 1-BETA; 1.
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; eEF-1beta-like; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR PROSITE; PS00824; EF1BD_1; 1.
DR PROSITE; PS00825; EF1BD_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768,
KW ECO:0000256|RuleBase:RU003791};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU003791};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640}.
FT DOMAIN 108..134
FT /note="Elongation factor 1 beta central acidic region
FT eukaryote"
FT /evidence="ECO:0000259|SMART:SM01182"
FT DOMAIN 143..229
FT /note="Translation elongation factor EF1B beta/delta
FT subunit guanine nucleotide exchange"
FT /evidence="ECO:0000259|SMART:SM00888"
FT REGION 67..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 229 AA; 24908 MW; A4E159BDB674E64B CRC64;
MGFGDLKAAS GLKVLNDFLS ARSYIEGFVP SQADVAVFEA ISTPPSADLC HALRWYNHIK
SYQDQKNSLP GVKKPLGQYG PAGVADTTPS SAPAAASKDD DDDDDIDLFG SDDEEDAEAA
KLKEQRLAEY AAKKAKKPAL IAKSSILLDV KPWDDETDMA KLEECVRSIQ MDGLVWGQSK
LVPVGYGIKK LQINCVVEDD KVGTDILEEQ ITAFEDYVQS MDVAAFNKI
//
