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Database: UniProt
Entry: A0A0L0LDZ0_9BACT
LinkDB: A0A0L0LDZ0_9BACT
Original site: A0A0L0LDZ0_9BACT 
ID   A0A0L0LDZ0_9BACT        Unreviewed;       161 AA.
AC   A0A0L0LDZ0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN   Name=pheS {ECO:0000313|EMBL:KND48194.1};
GN   ORFNames=AB201_01190 {ECO:0000313|EMBL:KND48194.1};
OS   Parcubacteria bacterium C7867-006.
OC   Bacteria; Candidatus Parcubacteria.
OX   NCBI_TaxID=1659200 {ECO:0000313|EMBL:KND48194.1, ECO:0000313|Proteomes:UP000037457};
RN   [1] {ECO:0000313|EMBL:KND48194.1, ECO:0000313|Proteomes:UP000037457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7867-006 {ECO:0000313|EMBL:KND48194.1};
RX   PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA   Nelson W.C., Stegen J.C.;
RT   "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT   symbiotic lifestyle.";
RL   Front. Microbiol. 6:713-713(2015).
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:0000256|ARBA:ARBA00000395};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KND48194.1}.
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DR   EMBL; LFCP01000001; KND48194.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0LDZ0; -.
DR   STRING; 1659200.AB201_01190; -.
DR   PATRIC; fig|1659200.3.peg.439; -.
DR   Proteomes; UP000037457; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0043039; P:tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00496; PheRS_alpha_core; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   PANTHER; PTHR11538:SF41; PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   4: Predicted;
KW   Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:KND48194.1};
KW   Ligase {ECO:0000313|EMBL:KND48194.1}.
FT   DOMAIN          1..140
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   161 AA;  18187 MW;  D628CE23482F420E CRC64;
     MEKNKPPIRI IAPGKVFRHE ATDATHEAQF YQLEGLVVGE NISVANLKWT LETMFEKLFG
     KKMNIRLRPS YFPFVEPGFE MDMSCFKCEG RGCSTCKNTG WIEIGGSGMV HPKVLESAGV
     DSKKYSGFAF GYGVDRIAML KYGIDDVRLL YQGDLRLVNQ F
//
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