ID   SYFAB_XENLA             Reviewed;         499 AA.
AC   Q7SYV0;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit B;
DE            EC=6.1.1.20 {ECO:0000250|UniProtKB:Q9Y285};
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit B;
DE            Short=PheRS;
GN   Name=farsa-b; Synonyms=farsla-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q9Y285};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:A5K9S0};
CC   -!- SUBUNIT: Heterotetramer; dimer of two heterodimers formed by alpha and
CC       beta subunits. {ECO:0000250|UniProtKB:Q9Y285}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q505J8}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Phe-tRNA synthetase alpha subunit type 2 subfamily. {ECO:0000305}.
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DR   EMBL; BC054256; AAH54256.1; -; mRNA.
DR   RefSeq; NP_001080851.1; NM_001087382.2.
DR   AlphaFoldDB; Q7SYV0; -.
DR   SMR; Q7SYV0; -.
DR   BioGRID; 98787; 1.
DR   IntAct; Q7SYV0; 1.
DR   DNASU; 380545; -.
DR   GeneID; 380545; -.
DR   KEGG; xla:380545; -.
DR   CTD; 380545; -.
DR   Xenbase; XB-GENE-6253419; farsa.L.
DR   OrthoDB; 733355at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 380545; Expressed in liver and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0009328; C:phenylalanine-tRNA ligase complex; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; ISS:UniProtKB.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; ISS:UniProtKB.
DR   GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR   Gene3D; 3.30.930.10; -; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR040724; PheRS_DBD1.
DR   InterPro; IPR040586; PheRS_DBD2.
DR   InterPro; IPR040725; PheRS_DBD3.
DR   Pfam; PF18552; PheRS_DBD1; 1.
DR   Pfam; PF18554; PheRS_DBD2; 1.
DR   Pfam; PF18553; PheRS_DBD3; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00468; pheS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..499
FT                   /note="Phenylalanine--tRNA ligase alpha subunit B"
FT                   /id="PRO_0000280453"
FT   BINDING         330
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         373..375
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         413
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         415
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000250|UniProtKB:A5K9S0"
FT   BINDING         439
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
SQ   SEQUENCE   499 AA;  56750 MW;  A632A4680B2C27C2 CRC64;
     MADNLLSEQL LQRLQDGDNK GVDTLELAAV LSVDHQQVVG AVKSLQCLGE IIEAEQRSSK
     KWELSSEGEE IAQVGSHEAR VFQSLPKEGL LQAELMKLPF AKVGFSKAMS NKWIRLDKAA
     AGGPCVYRVV ETIEDTVKEK LQLILKGRAD DVNEKDKNEL KKRKLVNEVT VKSYWVTKGS
     GFSTSITKQE TDLTPEMIAS GSWREKQFKG YNFNALGVMP ECGHLHPLLK VRTQFRQIFL
     EMGFTEMPTN NFIESSFWNF DALFQPQQHP ARDQHDTFFL QDPALATEFP MEYLERVKKV
     HSEGGYGSQG YKYDWSIHEA QKNILRTHTT AVSARMLYKL AHQKEFTPVK YFSIDRVFRN
     ETLDATHLAE FHQIEGVVAD RGLTLGNLMG VLKEFFHKLG ITKLRFKPAY NPYTEPSMEV
     FSYHEGLKKW VEVGNSGLFR PELLLPMGLP GDVNVLGWGL SLERPTMIRY GIKNIRELVG
     HKVNLQMVYD SPICRLDAC