ID   SYFB_NOSCE              Reviewed;         504 AA.
AC   C4VA52;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Probable phenylalanine--tRNA ligase beta subunit;
DE            EC=6.1.1.20;
DE   AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
DE            Short=PheRS;
GN   ORFNames=NCER_101490;
OS   Nosema ceranae (strain BRL01) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX   NCBI_TaxID=578460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRL01;
RX   PubMed=19503607; DOI=10.1371/journal.ppat.1000466;
RA   Cornman R.S., Chen Y.P., Schatz M.C., Street C., Zhao Y., Desany B.,
RA   Egholm M., Hutchison S., Pettis J.S., Lipkin W.I., Evans J.D.;
RT   "Genomic analyses of the microsporidian Nosema ceranae, an emergent
RT   pathogen of honey bees.";
RL   PLoS Pathog. 5:E1000466-E1000466(2009).
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         Evidence={ECO:0000250|UniProtKB:A5K464};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC       family. Type 2 subfamily. {ECO:0000305}.
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DR   EMBL; ACOL01000168; EEQ81893.1; -; Genomic_DNA.
DR   RefSeq; XP_002995564.1; XM_002995518.1.
DR   AlphaFoldDB; C4VA52; -.
DR   SMR; C4VA52; -.
DR   STRING; 578460.C4VA52; -.
DR   PRIDE; C4VA52; -.
DR   EnsemblFungi; EEQ81893; EEQ81893; NCER_101490.
DR   KEGG; nce:NCER_101490; -.
DR   VEuPathDB; MicrosporidiaDB:NCER_101490; -.
DR   HOGENOM; CLU_020279_2_0_1; -.
DR   InParanoid; C4VA52; -.
DR   OMA; FPGRCAN; -.
DR   Proteomes; UP000009082; Unassembled WGS sequence.
DR   GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IEA:EnsemblFungi.
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; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:EnsemblFungi.
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   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..504
FT                   /note="Probable phenylalanine--tRNA ligase beta subunit"
FT                   /id="PRO_0000388412"
FT   DOMAIN          270..346
FT                   /note="B5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT   BINDING         324
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         330
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         333
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         334
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   504 AA;  57671 MW;  C2718FAED9330A7D CRC64;
     MPTISVKKRE IEKLLGKSYD SETFSDILFN YGLEIDECIE ESDDITYKIE IPANRYDLLC
     AEGLNYALQS YLFGKVFEDI NLQSSEYTIF KQHFGNRSCV AAAIIKNYKF DKYSYDSFIS
     YQEKLCGNLG RNRSLVSMGT HDLDTISWPV TYKSIKKTEL KFAPLNCTKE INDLEMHFKD
     DKNIGKYLQY VDNDNYIVFM DAKGHILSVP PVINSNRTKI SVNTTNILVE VTGTNTYKVN
     TCLKMILSAF RTDNMCQVNI ISDKQEILEI KDKSYLLSID EVYKELNINI SVIDLSDLLI
     KMMYKTNIID DKHLNVTVPS VRQDVLHKAD LIEDIAICYG FNNINMVMPD INTIGSENRL
     NKFSDKLRLE MCMLGFTEVY TMVLVSKSDN IFGDNSAVVS NYKSLECEAV RSSLYPGLMK
     AVSSNLHCKI PIKIFEVGDV VFLDSESDVG ARNRRYLSCL YVGNKSHLED VQGPMTVILE
     KCGIKDYKFE RMDDEKKYLK NQSA