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Database: UniProt
Entry: A0A3Q1AKV2_AMPOC
LinkDB: A0A3Q1AKV2_AMPOC
Original site: A0A3Q1AKV2_AMPOC 
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
//
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