ID A0A0G1NDQ7_9BACT Unreviewed; 399 AA.
AC A0A0G1NDQ7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=UW92_C0015G0002 {ECO:0000313|EMBL:KKT91252.1};
OS Candidatus Jorgensenbacteria bacterium GW2011_GWA2_45_13.
OC Bacteria; Candidatus Jorgensenbacteria.
OX NCBI_TaxID=1618662 {ECO:0000313|EMBL:KKT91252.1, ECO:0000313|Proteomes:UP000033966};
RN [1] {ECO:0000313|EMBL:KKT91252.1, ECO:0000313|Proteomes:UP000033966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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 -!- 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:KKT91252.1}.
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DR EMBL; LCKF01000015; KKT91252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1NDQ7; -.
DR PATRIC; fig|1618662.3.peg.328; -.
DR Proteomes; UP000033966; 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; 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 142..275
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT DOMAIN 291..399
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
SQ SEQUENCE 399 AA; 45185 MW; BDC629BD00FB9401 CRC64;
MTSLERAKLE VQKENPNLPM EPKFEVSSPE TIEKLLSVED LTLPSREGQE RNIVGRVYDQ
VLTKLTEHNF PNINVIRGNS TVDVKDNFDK LLFSPGNPGR SSTYTRYVDG DHILRTHTSA
LIPSTFENLE KNIDQATFVL PGLVYRRDVI DPKHLDVFHQ IDVWTLQKNK AHGRVSRENL
LELAKTVFEA ACPGAKMIVY EAKHPYTIDG IEVYAGVDGK EIEVFEAGLA HPDVLKNSGI
DPEEYSGLAL GMGVERLIMA RKNLPDIRLI RSTDPRVVKQ MTNMEKFKDV SDKPAIARDM
SYCVNKNDTE EDICEAIRDA FGDKSDLLEQ VEVLERTPFD KLNPIAKERL GAKEDQDNVL
VRIILRHPDK TLTKKESAEL YSKAYPKLHK GTTKGYEVK
//
