ID A0A3D0JCS2_9FIRM Unreviewed; 300 AA. AC A0A3D0JCS2; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 13-FEB-2019, entry version 2. DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000256|SAAS:SAAS00710993}; DE EC=6.1.1.20 {ECO:0000256|SAAS:SAAS00710991}; DE Flags: Fragment; GN ORFNames=DEO81_06790 {ECO:0000313|EMBL:HBZ89076.1}; OS Erysipelotrichaceae bacterium. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae. OX NCBI_TaxID=2049044 {ECO:0000313|EMBL:HBZ89076.1}; RN [1] {ECO:0000313|EMBL:HBZ89076.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBA9793 {ECO:0000313|EMBL:HBZ89076.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny RT substantially revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + CC H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, CC Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; CC EC=6.1.1.20; Evidence={ECO:0000256|SAAS:SAAS01116698}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|SAAS:SAAS00710989}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000256|SAAS:SAAS00710972}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00710994}. CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta CC subunit family. Type 1 subfamily. {ECO:0000256|SAAS:SAAS00710957}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:HBZ89076.1}. 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; DOVK01000169; HBZ89076.1; -; Genomic_DNA. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR CDD; cd02796; tRNA_bind_bactPheRS; 1. DR Gene3D; 3.50.40.10; -; 1. DR InterPro; IPR005146; B3/B4_tRNA-bd. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR020825; Phe-tRNA_synthase_B3/B4. DR InterPro; IPR002547; tRNA-bd_dom. DR InterPro; IPR033714; tRNA_bind_bactPheRS. DR Pfam; PF03483; B3_4; 1. DR Pfam; PF01588; tRNA_bind; 1. DR SMART; SM00873; B3_4; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR PROSITE; PS50886; TRBD; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|SAAS:SAAS00710960}; KW ATP-binding {ECO:0000256|SAAS:SAAS00710992}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00710959}; KW Ligase {ECO:0000256|SAAS:SAAS00710995, ECO:0000313|EMBL:HBZ89076.1}; KW Magnesium {ECO:0000256|SAAS:SAAS00710979}; KW Metal-binding {ECO:0000256|SAAS:SAAS00710958}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00710997}; KW Protein biosynthesis {ECO:0000256|SAAS:SAAS00710967}; KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00209, KW ECO:0000256|SAAS:SAAS00514389}; KW tRNA-binding {ECO:0000256|PROSITE-ProRule:PRU00209, KW ECO:0000256|SAAS:SAAS00514462}. FT DOMAIN 39 152 TRNA-binding. {ECO:0000259|PROSITE: FT PS50886}. FT NON_TER 300 300 {ECO:0000313|EMBL:HBZ89076.1}. SQ SEQUENCE 300 AA; 33818 MW; 5B3C32B2E11B0F7F CRC64; MLASYKLLNQ YVKVDDQNPE ELAEKITRIG HEVEGHYPLA LGTKLVVGYV KECIDHPDSD HLHVCKVNIG TETIQIVCGA SNVRVGIKVI VALPGAVLPG DFEIKKGKIR GVESNGMICA LFELGLEEKT EENYNKGIEE LPLDAPVGKD ALEYLDVEDT LYELDVHKHR NNDCYYHIGF AHEIGTVLDK KVNYPEAKYN EIDDDVNNYI KLTVETERCP YYLGKMVRNV KIGESPEWIK KRLIAAGMRP INNVVDISNF VMLEYGQPTH FFDADKLGNT VLVRDAKDNE EITTLDGIKR //