ID A0A1F6C1V0_9BACT Unreviewed; 383 AA.
AC A0A1F6C1V0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
DE AltName: Full=Phenylalanyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031194};
GN ORFNames=A3G50_01285 {ECO:0000313|EMBL:OGG43174.1};
OS Candidatus Jorgensenbacteria bacterium RIFCSPLOWO2_12_FULL_42_11.
OC Bacteria; Candidatus Jorgensenbacteria.
OX NCBI_TaxID=1798473 {ECO:0000313|EMBL:OGG43174.1, ECO:0000313|Proteomes:UP000176633};
RN [1] {ECO:0000313|EMBL:OGG43174.1, ECO:0000313|Proteomes:UP000176633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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:OGG43174.1}.
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DR EMBL; MFKM01000021; OGG43174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6C1V0; -.
DR STRING; 1798473.A3G50_01285; -.
DR Proteomes; UP000176633; 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 Gene3D; 3.30.70.380; Ferrodoxin-fold anticodon-binding domain; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005121; Fdx_antiC-bd.
DR InterPro; IPR036690; Fdx_antiC-bd_sf.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR PANTHER; PTHR11538:SF41; PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03147; FDX-ACB; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SMART; SM00896; FDX-ACB; 1.
DR SUPFAM; SSF54991; Anticodon-binding domain of PheRS; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51447; FDX_ACB; 1.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 138..292
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT DOMAIN 289..383
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
SQ SEQUENCE 383 AA; 44736 MW; CF1408F3528CBDC9 CRC64;
MSTKRRNLTI NDPEMPAVLS KLQNKTDFKS LRIKQLLALP DLTKTNDSPI KFLIDAIVNL
RRFKNFDIIN VPEIVSVRNN FDLLNAPADH PSRQETDTYY PEKDWVLRTH TTVMWPYYFS
EENMKKLETE GEIGALCFGK VYRKDEIDRS HYPAFHQIDG LYICRKDKKI IGILELTEVL
VDIAKNIYGT DVEYQISEDT FPFTDPSLQI AIKGKNQWLE IVGAGVVHTR VLKNLDIDPS
VYNGWAFGFG LERLAMIKME IPDIRIFWST DKRITGQFKD LNSRFQEISK YPMTYRDISF
VVGKDTSLNN YYEIIRDCAG NLVEEVSLLD KYENKEKFGE NNISYTFHIV YRSNERTLTN
DEVDKIQRLL IDRTRKELNA LVR
//
