SYFB_CAEEL
ID SYFB_CAEEL Reviewed; 591 AA.
AC Q19713;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit;
DE EC=6.1.1.20;
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
DE Short=PheRS;
GN Name=fars-3 {ECO:0000312|WormBase:F22B5.9};
GN Synonyms=frs-2 {ECO:0000312|WormBase:F22B5.9};
GN ORFNames=F22B5.9 {ECO:0000312|WormBase:F22B5.9};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +
CC L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668,
CC Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A5K464};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 2 subfamily. {ECO:0000305}.
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DR EMBL; Z50044; CAA90360.1; -; Genomic_DNA.
DR PIR; T21245; T21245.
DR RefSeq; NP_495785.1; NM_063384.6.
DR AlphaFoldDB; Q19713; -.
DR SMR; Q19713; -.
DR BioGRID; 39680; 5.
DR IntAct; Q19713; 4.
DR STRING; 6239.F22B5.9; -.
DR World-2DPAGE; 0011:Q19713; -.
DR EPD; Q19713; -.
DR PaxDb; Q19713; -.
DR PeptideAtlas; Q19713; -.
DR EnsemblMetazoa; F22B5.9.1; F22B5.9.1; WBGene00001498.
DR GeneID; 174351; -.
DR KEGG; cel:CELE_F22B5.9; -.
DR UCSC; F22B5.9; c. elegans.
DR CTD; 174351; -.
DR WormBase; F22B5.9; CE20708; WBGene00001498; fars-3.
DR eggNOG; KOG2472; Eukaryota.
DR GeneTree; ENSGT00530000063489; -.
DR HOGENOM; CLU_020279_2_0_1; -.
DR InParanoid; Q19713; -.
DR OMA; FPGRCAN; -.
DR OrthoDB; 378921at2759; -.
DR PhylomeDB; Q19713; -.
DR PRO; PR:Q19713; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001498; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IBA:GO_Central.
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:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00769; PheRS_beta_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.50.40.10; -; 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; 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; IPR005147; tRNA_synthase_B5-dom.
DR PANTHER; PTHR10947; PTHR10947; 1.
DR Pfam; PF03483; B3_4; 1.
DR Pfam; PF03484; B5; 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 SUPFAM; SSF46955; SSF46955; 2.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00471; pheT_arch; 1.
DR PROSITE; PS51483; B5; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..591
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000127018"
FT DOMAIN 304..380
FT /note="B5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT BINDING 358
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT BINDING 367
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT BINDING 368
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
SQ SEQUENCE 591 AA; 66062 MW; 3965719A5FBC52F8 CRC64;
MPTVGIKKVI LDKHFKRVYS EKEFDELCFE YGLELDEITS EKAAVEKEQG TRAASDLNDQ
EVYKIDIPAN RYDLLSVEGL ARAIRIFKQE IPSPAYKYAD VPKTGLQKII VKKETAQVRP
FVVGAVLRDI SFDADSYASF IDLQDKLHQN ICRKRTLVAI GTHDLDTIQG PFEYRAEAPK
DIKFKPLNQT KEYTAEELMT LYSTDSHLKA YLPIIQNHPV YPVIYDKNGV VCSMPPIING
EHSKITLNTK NVFIEATATD KQKAFVVLDT IVTLFSQYCA KPFTIEQVEV VYEETGVKEL
YPLLSYREMT VTTPEINTKI GINLKDEEMA TLLNKMSLKA EVAAKETLKI VVPPTRHDIL
HACDIAEDVG VAFGYNNLIT KLPESNTVAV AFPINKLCDN LRIEIAAAGW TEALNFALCS
RDDISSKLRQ PDALSHAVHI GNPKTLEFQV ARTSLLPGLL KTLSSNRDMP LPLKLFELQD
VIVKDSNTDV GARNERRLAA VYYNRAAGFE IIQGFLDRIM RMLNVNPARD GTGYYIEADE
NSTYFPGRCA KIIGPKGVVL GHIGALHPEV ITSFGLTLPC GAVEINVEPF L
