ID SYFB_THETH Reviewed; 785 AA. AC P27002; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 2. DT 24-JAN-2024, entry version 157. 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=pheT; OS Thermus thermophilus. OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=274; RN [1] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=10092459; DOI=10.1006/jmbi.1999.2617; RA Reshetnikova L., Moor N., Lavrik O., Vassylyev D.G.; RT "Crystal structures of phenylalanyl-tRNA synthetase complexed with RT phenylalanine and a phenylalanyl-adenylate analogue."; RL J. Mol. Biol. 287:555-568(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 -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 2 magnesium ions per tetramer.; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit CC family. Type 1 subfamily. {ECO:0000305}. CC -!- CAUTION: The sequence shown here has been extracted from PDB entry CC 1B70. {ECO:0000305}. 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 RefSeq; WP_011229047.1; NZ_DFSU01000029.1. DR PDB; 1B70; X-ray; 2.70 A; B=1-785. DR PDB; 1B7Y; X-ray; 2.50 A; B=1-785. DR PDB; 2AKW; X-ray; 2.80 A; B=1-785. DR PDB; 2ALY; X-ray; 2.60 A; B=1-785. DR PDB; 2AMC; X-ray; 2.70 A; B=1-785. DR PDB; 2IY5; X-ray; 3.10 A; B=1-785. DR PDB; 3TEH; X-ray; 2.85 A; B=1-785. DR PDB; 4TVA; X-ray; 2.60 A; B=1-785. DR PDBsum; 1B70; -. DR PDBsum; 1B7Y; -. DR PDBsum; 2AKW; -. DR PDBsum; 2ALY; -. DR PDBsum; 2AMC; -. DR PDBsum; 2IY5; -. DR PDBsum; 3TEH; -. DR PDBsum; 4TVA; -. DR AlphaFoldDB; P27002; -. DR SMR; P27002; -. DR DIP; DIP-6105N; -. DR MINT; P27002; -. DR GeneID; 3169713; -. DR EvolutionaryTrace; P27002; -. 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:UniProtKB-UniRule. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00769; PheRS_beta_core; 1. DR CDD; cd02796; tRNA_bind_bactPheRS; 1. DR Gene3D; 3.30.56.10; -; 2. DR Gene3D; 3.30.70.380; Ferrodoxin-fold anticodon-binding domain; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 1. DR HAMAP; MF_00283; Phe_tRNA_synth_beta1; 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; IPR005121; Fdx_antiC-bd. DR InterPro; IPR036690; Fdx_antiC-bd_sf. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu. DR InterPro; IPR004532; Phe-tRNA-ligase_IIc_bsu_bact. DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4. DR InterPro; IPR041616; PheRS_beta_core. DR InterPro; IPR002547; tRNA-bd_dom. DR InterPro; IPR033714; tRNA_bind_bactPheRS. DR InterPro; IPR005147; tRNA_synthase_B5-dom. DR NCBIfam; TIGR00472; pheT_bact; 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; PF03147; FDX-ACB; 1. DR Pfam; PF17759; tRNA_synthFbeta; 1. DR SMART; SM00873; B3_4; 1. DR SMART; SM00874; B5; 1. DR SMART; SM00896; FDX-ACB; 1. DR SUPFAM; SSF54991; Anticodon-binding domain of PheRS; 1. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR SUPFAM; SSF56037; PheT/TilS domain; 1. DR SUPFAM; SSF46955; Putative DNA-binding domain; 2. DR PROSITE; PS51483; B5; 1. DR PROSITE; PS51447; FDX_ACB; 1. DR PROSITE; PS50886; TRBD; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW RNA-binding; tRNA-binding. FT CHAIN 1..785 FT /note="Phenylalanine--tRNA ligase beta subunit" FT /id="PRO_0000126978" FT DOMAIN 39..147 FT /note="tRNA-binding" FT DOMAIN 399..474 FT /note="B5" FT DOMAIN 688..780 FT /note="FDX-ACB" FT BINDING 452 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT BINDING 458 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT BINDING 461 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT BINDING 462 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with alpha subunit" FT STRAND 2..4 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 5..8 FT /evidence="ECO:0007829|PDB:1B7Y" FT TURN 9..11 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 18..28 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 34..37 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 45..55 FT /evidence="ECO:0007829|PDB:1B7Y" FT TURN 57..60 FT /evidence="ECO:0007829|PDB:1B70" FT STRAND 62..76 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 86..90 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:3TEH" FT STRAND 105..108 FT /evidence="ECO:0007829|PDB:3TEH" FT STRAND 109..113 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 115..117 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 120..123 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 154..157 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 165..168 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 170..179 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 199..205 FT /evidence="ECO:0007829|PDB:1B7Y" FT TURN 207..209 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 211..220 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 228..236 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 244..255 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 261..264 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 265..267 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 271..276 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 282..285 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 290..292 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 298..304 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 307..313 FT /evidence="ECO:0007829|PDB:1B7Y" FT TURN 314..316 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 317..319 FT /evidence="ECO:0007829|PDB:1B7Y" FT TURN 320..322 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 330..337 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 340..349 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 355..362 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 369..383 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 387..390 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 393..395 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 404..406 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 408..415 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 421..430 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 434..445 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 456..467 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 469..471 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 483..485 FT /evidence="ECO:0007829|PDB:1B7Y" FT TURN 486..489 FT /evidence="ECO:0007829|PDB:3TEH" FT HELIX 490..505 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 514..516 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 520..523 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 532..535 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 541..544 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 549..562 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 568..592 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 597..600 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 606..620 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 625..627 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 634..644 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 647..655 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 657..662 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 669..676 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 693..697 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 701..705 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 707..718 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 722..729 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 737..739 FT /evidence="ECO:0007829|PDB:3TEH" FT STRAND 744..749 FT /evidence="ECO:0007829|PDB:1B7Y" FT STRAND 752..754 FT /evidence="ECO:0007829|PDB:1B7Y" FT HELIX 758..773 FT /evidence="ECO:0007829|PDB:1B7Y" FT TURN 774..776 FT /evidence="ECO:0007829|PDB:3TEH" SQ SEQUENCE 785 AA; 86611 MW; BDC51952DE8E0F00 CRC64; MRVPFSWLKA YVPELESPEV LEERLAGLGF ETDRIERVFP IPRGVVFARV LEAHPIPGTR LKRLVLDAGR TVEVVSGAEN ARKGIGVALA LPGTELPGLG QKVGERVIQG VRSFGMALSP RELGVGEYGG GLLEFPEDAL PPGTPLSEAW PEEVVLDLEV TPNRPDALGL LGLARDLHAL GYALVEPEAA LKAEALPLPF ALKVEDPEGA PHFTLGYAFG LRVAPSPLWM QRALFAAGMR PINNVVDVTN YVMLERAQPM HAFDLRFVGE GIAVRRAREG ERLKTLDGVE RTLHPEDLVI AGWRGEESFP LGLAGVMGGA ESEVREDTEA IALEVACFDP VSIRKTARRH GLRTEASHRF ERGVDPLGQV PAQRRALSLL QALAGARVAE ALLEAGSPKP PEAIPFRPEY ANRLLGTSYP EAEQIAILKR LGCRVEGEGP TYRVTPPSHR LDLRLEEDLV EEVARIQGYE TIPLALPAFF PAPDNRGVEA PYRKEQRLRE VLSGLGFQEV YTYSFMDPED ARRFRLDPPR LLLLNPLAPE KAALRTHLFP GLVRVLKENL DLDRPERALL FEVGRVFRER EETHLAGLLF GEGVGLPWAK ERLSGYFLLK GYLEALFARL GLAFRVEAQA FPFLHPGVSG RVLVEGEEVG FLGALHPEIA QELELPPVHL FELRLPLPDK PLAFQDPSRH PAAFRDLAVV VPAPTPYGEV EALVREAAGP YLESLALFDL YQGPPLPEGH KSLAFHLRFR HPKRTLRDEE VEEAVSRVAE ALRARGFGLR GLDTP //