ID A0A3Q1AKV2_AMPOC Unreviewed; 848 AA.
AC A0A3Q1AKV2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Elongation factor 1-beta {ECO:0000256|ARBA:ARBA00017600};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
DE AltName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000256|ARBA:ARBA00017032};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000001807.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000001807.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 2 subfamily. {ECO:0000256|ARBA:ARBA00007438}.
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DR AlphaFoldDB; A0A3Q1AKV2; -.
DR STRING; 80972.ENSAOCP00000001807; -.
DR Ensembl; ENSAOCT00000012585.1; ENSAOCP00000001807.1; ENSAOCG00000004912.1.
DR GeneTree; ENSGT00530000063489; -.
DR OrthoDB; 5473299at2759; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00292; EF1B; 1.
DR CDD; cd00769; PheRS_beta_core; 1.
DR Gene3D; 1.20.1050.130; -; 1.
DR Gene3D; 3.30.56.10; -; 2.
DR Gene3D; 3.30.70.60; -; 1.
DR Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005146; B3/B4_tRNA-bd.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
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; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR InterPro; IPR004531; Phe-tRNA-synth_IIc_bsu_arc_euk.
DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR InterPro; IPR041616; PheRS_beta_core.
DR InterPro; IPR040659; PhetRS_B1.
DR InterPro; IPR014717; Transl_elong_EF1B/ribsomal_bS6.
DR InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR InterPro; IPR005147; tRNA_synthase_B5-dom.
DR NCBIfam; TIGR00471; pheT_arch; 1.
DR PANTHER; PTHR10947:SF0; PHENYLALANINE--TRNA LIGASE BETA SUBUNIT; 1.
DR PANTHER; PTHR10947; PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47; 1.
DR Pfam; PF03483; B3_4; 1.
DR Pfam; PF03484; B5; 1.
DR Pfam; PF10587; EF-1_beta_acid; 1.
DR Pfam; PF00736; EF1_GNE; 1.
DR Pfam; PF18262; PhetRS_B1; 1.
DR Pfam; PF17759; tRNA_synthFbeta; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SMART; SM01182; EF-1_beta_acid; 2.
DR SMART; SM00888; EF1_GNE; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF54984; eEF-1beta-like; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF56037; PheT/TilS domain; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 2.
DR PROSITE; PS51483; B5; 1.
DR PROSITE; PS00824; EF1BD_1; 1.
DR PROSITE; PS00825; EF1BD_2; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768,
KW ECO:0000256|RuleBase:RU003791}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU003791};
KW Reference proteome {ECO:0000313|Proteomes:UP000257160}.
FT DOMAIN 303..380
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
SQ SEQUENCE 848 AA; 94707 MW; 480FD8D6DC47D615 CRC64;
MPTVGIKRDL LFKALGRTYT DEEFDELCFE FGLELDEITS EKEIVSREQG DTKASDASDV
ILYKIDVPAN RYDLLCLEGL VRGLQVFKNK LEAPRYRRIS PVNGDPQKLI ITKETAAVRP
FAVAAVLRNI TFTQERYDSF IELQEKLHQN ICRKRSLVAI GTHDLDTISG PFTYTAKPPG
DISFKPLNQT KEYTATELMS LYKTDSHLRH YLHIIEDKPV YPIIYDSKGI VLSMPPIING
DHSKITLQTK NVFIECTATD LTKAKIVLDM MVTMFSEYCS QPFTVEEAEV VYPDGKTCIY
PELAYRKEKL SGEFINRKVG INESTEKIAQ LLTRMCLLSR ATGVGDEIEV EIPPTRSDVI
HACDIMEDAA IAYGFNNITR TTPRAYTVAN QFPLNKLTEL LRQDLAAAGF TEALNFALCS
EEDIADKLGK KISETRAAHI SNPKTAEFQV ARTTLLPGLL KTIAANRKMP LPLKLFEVSD
VVLKDETKDV GARNSRRFCA VYYNKSPGFE VIHGLLDRTM QLLEVKSARG EGYHIQAADD
STFFPGRCAE IIVRGKTVGR LGVLHPDVIN RFELTMPCSA MEIDIEPFLG HTAETLLTHD
VPMQEVIKHK FPTPDESQQA PVSRPTSTKT VFGDVSTQVG LKALNDFLAD KSYMEGFAAS
QADMTVFDAI PSPPSLTFCH LRRWYNHIKS FQRERARLPA AKRQFVLPAA PAASTNNASD
DDDIDLFGSD DEAESAEAAR VKERRLAEYA AKKSKKPALI AKSSILLDVK PWDDETDMAK
LEECVRSVSM DGLLWGQSKL VPVGYGIKKL QIGCVVEDDK VGTDLLEEAI TAFEDYVQSV
DVAAFNKI
//