ID A0A448YID2_BRENA Unreviewed; 591 AA.
AC A0A448YID2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN ORFNames=BRENAR_LOCUS1424 {ECO:0000313|EMBL:VEU20689.1};
OS Brettanomyces naardenensis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Brettanomyces.
OX NCBI_TaxID=13370 {ECO:0000313|EMBL:VEU20689.1, ECO:0000313|Proteomes:UP000290900};
RN [1] {ECO:0000313|EMBL:VEU20689.1, ECO:0000313|Proteomes:UP000290900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tiukova I., Dainat J.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|ARBA:ARBA00011209}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 2 subfamily. {ECO:0000256|ARBA:ARBA00007438}.
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DR EMBL; CAACVR010000006; VEU20689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A448YID2; -.
DR STRING; 13370.A0A448YID2; -.
DR InParanoid; A0A448YID2; -.
DR Proteomes; UP000290900; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:InterPro.
DR CDD; cd00769; PheRS_beta_core; 1.
DR Gene3D; 3.30.56.10; -; 2.
DR Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 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 NCBIfam; TIGR00471; pheT_arch; 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; PF18262; PhetRS_B1; 1.
DR Pfam; PF17759; tRNA_synthFbeta; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF56037; PheT/TilS domain; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 2.
DR PROSITE; PS51483; B5; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000290900}.
FT DOMAIN 291..369
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
SQ SEQUENCE 591 AA; 66592 MW; 603DE8217AE2AC62 CRC64;
MPTVAVDKQD LFDLLGRNYT HKEFDELCFD FGIELDEDTT DDVAGTDERP EYKIEIAANR
YDMLCIEGIA QALNEYLGNT DTPKYTLKPA EPEISLTIDQ STEEIRPYAC SAILRNVKFN
QRNYDSFIAL QDKLHTNICR QRTLVAIGTH DLDTIKPPFF YKALAPEKIK FAPLNQTEVM
DGNRLMEFYE NDKNLGRYLH IIRDSPVYPV VLDSNGTVCS LPPIINGNHS KISLNTKNVF
IEVTATDKTK AEVVINQIVA MFSRYCDDKF SIEPVKIISE HNGQTRVCPN IKPRNMPAEK
DYINSCLALD LSTDEIRKLL KKMSLPAKGS TTDGNIINVS VPITRPDILH QCDVMEDCAI
SYGYNNLKKT SPKTVATTAH PLPINKVSDI LRTASAQAGW LEVMPLTLCS HKENFENLKA
VDDNTKAVKL ENPKTVEYQV VRTTLVPGIL KTIKENKRHS LPIKVFEAGD IVLKDDSLER
KARNQRNWCA AYAGKVSGFE LIQGLLGKVM QTFRTPWLED PTTGEHGFWL VESDDKKMYF
PGRGAKIMLR AKKGKESVEI GHIGVLHPEV VTNFEIPFAV STVEINSEIF L
//
