ID SYFB_PYRFU Reviewed; 556 AA. AC Q8U260; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 110. DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00284}; DE EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00284}; DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00284}; DE Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00284}; GN Name=pheT {ECO:0000255|HAMAP-Rule:MF_00284}; OrderedLocusNames=PF0990; OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=186497; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299; RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., RA DiRuggiero J., Robb F.T.; RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. RT horikoshii inferred from complete genomic sequences."; RL Genetics 152:1299-1305(1999). 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 Evidence={ECO:0000255|HAMAP-Rule:MF_00284}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00284}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000255|HAMAP-Rule:MF_00284}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00284}. CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit CC family. Type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00284}. 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; AE009950; AAL81114.1; -; Genomic_DNA. DR RefSeq; WP_011012127.1; NZ_CP023154.1. DR AlphaFoldDB; Q8U260; -. DR SMR; Q8U260; -. DR IntAct; Q8U260; 1. DR STRING; 186497.PF0990; -. DR PaxDb; 186497-PF0990; -. DR GeneID; 41712803; -. DR KEGG; pfu:PF0990; -. DR PATRIC; fig|186497.12.peg.1049; -. DR eggNOG; arCOG00412; Archaea. DR HOGENOM; CLU_020279_3_0_2; -. DR OrthoDB; 10073at2157; -. DR PhylomeDB; Q8U260; -. DR Proteomes; UP000001013; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00769; PheRS_beta_core; 1. DR Gene3D; 3.30.56.10; -; 2. DR Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 1. DR HAMAP; MF_00284; Phe_tRNA_synth_beta2; 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; IPR022918; Phe_tRNA_ligase_beta2_arc. DR InterPro; IPR041616; PheRS_beta_core. 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; PF17759; tRNA_synthFbeta; 1. DR SMART; SM00873; B3_4; 1. DR SMART; SM00874; B5; 1. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF56037; PheT/TilS domain; 1. DR SUPFAM; SSF46955; Putative DNA-binding domain; 2. 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..556 FT /note="Phenylalanine--tRNA ligase beta subunit" FT /id="PRO_0000127008" FT DOMAIN 278..354 FT /note="B5" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284" FT BINDING 332 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284" FT BINDING 338 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284" FT BINDING 341 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284" FT BINDING 342 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00284" SQ SEQUENCE 556 AA; 63963 MW; CFFB32F60D001432 CRC64; MPKFDVAKSD LERLVGREFS VEEWEDLVLY AKCELDDVWE EDGKIYFKLD SKDTNRPDLW SAEGVARQIR WALGLAKGLP KYEVEESDVV VYVDKKLRNI RPYGVYAVVE GLKLDEEALS QLIQLQEKVA LTYGRRRREV AIGIFDFDKV KPPIYYRAAE KTEKFVPLGY SEEMTLEEIL EKHEKGREYG HLIRDKPYYP LLVDSEGNVL SMPPIINSEL TGRVTTETKN VFVDVTGWDL RKVMLALNVI VTALAERGGK IKRVKVIYPD FEITTPDLTP KEFEVSFEYI RKLSGLELSN EEIKELLERM MYEVEILSEN KAKVKYPAFR DDIMHTRDVL EDVLIAYGYN NIDPEEPKLA VQGRGDPFKD FEDAIRDLMV GFGLQEVMTF NLTSKEVQFD KMNIPEEEIV EIANPISSRW SALRKWLLPS LMEFLSNNTH EEYPQRIFEV GLATLIDESR ETKTVSEPKL AVALAGSGYT FTNAKEILDS LMRHLGIEYD IEETVHGSFI PGRVGKILVD GKEIGIIGEI HPQVLENWNI QVPVVAFEIF LKPLYR //