ID V7PWS9_9BACT Unreviewed; 240 AA.
AC V7PWS9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:ETB63580.1};
GN ORFNames=O210_OD1C00001G0033 {ECO:0000313|EMBL:ETB63580.1};
OS Parcubacteria bacterium RAAC4_OD1_1.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1394712 {ECO:0000313|EMBL:ETB63580.1, ECO:0000313|Proteomes:UP000018547};
RN [1] {ECO:0000313|EMBL:ETB63580.1, ECO:0000313|Proteomes:UP000018547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kantor R.S., Wrighton K.C., Handley K.M., Sharon I., Hug L.A.,
RA Castelle C.J., Thomas B.C., Banfield J.F.;
RT "Small genomes and sparse metabolisms of sediment-associated bacteria from
RT four candidate phyla.";
RL Submitted (NOV-2013) 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: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:ETB63580.1}.
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DR EMBL; AWSN01000001; ETB63580.1; -; Genomic_DNA.
DR AlphaFoldDB; V7PWS9; -.
DR STRING; 1394712.O210_OD1C00001G0033; -.
DR PATRIC; fig|1394712.3.peg.35; -.
DR Proteomes; UP000018547; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-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; IPR004529; Phe-tRNA-synth_IIc_asu.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR NCBIfam; TIGR00468; pheS; 1.
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:ETB63580.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000313|EMBL:ETB63580.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018547}.
FT DOMAIN 19..220
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 240 AA; 27546 MW; BD26EB945701E072 CRC64;
MEEDIKKYKK GSLHPLTLIT NEAVSIFKDL GFVVEVGPEL EDEWYNFDAL NVPKDHPARD
MQDTFFIKGQ KEKVLRTHTS NTQIRFMEEL VKSGGVPPFA IVVPGKVFRN ESTDVTHEMQ
FYQIEGLMIG EDISVAHMKG VLLEFFKRFF DGEEVDIRLR PSFFPFVEPG FEIDLKKGDK
WIELLGAGMV HPNVLKNCGI DGEKYQGFAF GIGLDRLMMM KLKISDVRLS YQGDLRLNQF
//
