ID   SYFB_PONAB              Reviewed;         589 AA.
AC   Q5R7F7;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Phenylalanine--tRNA ligase beta subunit;
DE            EC=6.1.1.20 {ECO:0000250|UniProtKB:Q9NSD9};
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
DE            Short=PheRS;
GN   Name=FARSB; Synonyms=FARSLB;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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:Q9NSD9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19414;
CC         Evidence={ECO:0000250|UniProtKB:Q9NSD9};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:A5K464};
CC   -!- SUBUNIT: Heterotetramer; dimer of two heterodimers formed by FARSA and
CC       FARSB. {ECO:0000250|UniProtKB:Q9NSD9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NSD9}.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC       family. Type 2 subfamily. {ECO:0000305}.
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DR   EMBL; CR860161; CAH92303.1; -; mRNA.
DR   AlphaFoldDB; Q5R7F7; -.
DR   SMR; Q5R7F7; -.
DR   STRING; 9601.ENSPPYP00000014775; -.
DR   eggNOG; KOG2472; Eukaryota.
DR   InParanoid; Q5R7F7; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0009328; C:phenylalanine-tRNA ligase complex; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; ISS:UniProtKB.
DR   GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
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   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   CHAIN           1..589
FT                   /note="Phenylalanine--tRNA ligase beta subunit"
FT                   /id="PRO_0000284443"
FT   DOMAIN          302..379
FT                   /note="B5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT   BINDING         357
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         363
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         366
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"
SQ   SEQUENCE   589 AA;  66092 MW;  6767C75AB5DE8C01 CRC64;
     MPTVSVKRDL LFQALGRTYT DEEFDELCFE FGLELDEITS EKEIISKEQG NVKAAGASDV
     VLYKIDVPAN RYDLLCLEGL VRGLQVFKER IKAPVYKRVM PDGKIQKLII TEETAKIRPF
     AVAAVLRNIK FTKDRYDSFI ELQEKLHQNI CRKRALVAIG THDLDTLSGP FTYTAKRPSD
     IKFKPLNKTK EYTACELMNI YKTDNHLKHY LHIIENKPLY PVIYDSNGVV LSMPPIINGD
     HSRITVNTRN IFIECTGTDF TKAKIVLDII VTMFSEYCEN QFTVEAAEVV FPNGKSHTFP
     ELAYRKEMVR ADLINKKVGI RETPENLAKL LTRMYLKSEV IGDGNQIEIE IPPTRADIIH
     ACDIVEDAAI AYGYSNIQMT LPKTYTIANQ FPLNKLTELL RHDMAAAGFT EALTFALCSQ
     EDIADKLGVD ISATKAVHIS SPKTAEFQVA RTTLLPGLLK TIAANRKMPL PLKLFEISDI
     VIKDSNTDVG AKNYRHLCAV YYNKNPGFEI IHGLLDRIMQ LLDVLPGEDK GGYVIKASEG
     PAFFPGRCAE IFARGQSVGK LGVLHPDVIT KFELTMPCSS LEINIGPFL