ID A0A0G0MQ30_9BACT Unreviewed; 400 AA.
AC A0A0G0MQ30;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=US88_C0016G0023 {ECO:0000313|EMBL:KKQ67051.1};
OS Parcubacteria group bacterium GW2011_GWA2_38_27.
OC Bacteria.
OX NCBI_TaxID=1618812 {ECO:0000313|EMBL:KKQ67051.1, ECO:0000313|Proteomes:UP000034280};
RN [1] {ECO:0000313|EMBL:KKQ67051.1, ECO:0000313|Proteomes:UP000034280}
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:KKQ67051.1}.
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DR EMBL; LBUR01000016; KKQ67051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0MQ30; -.
DR STRING; 1618812.US88_C0016G0023; -.
DR PATRIC; fig|1618812.3.peg.636; -.
DR Proteomes; UP000034280; 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 156..309
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT DOMAIN 306..400
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
SQ SEQUENCE 400 AA; 46499 MW; E0808D90314C139E CRC64;
MEKINYSDYQ KTGDSDGERR VIVVKDLNNE KLISEIRNNA ATDTNSARIK RLLDLPDLSR
KEGSPIKFII DKILDIPSFK DFDVIEIPEI VDVAKNFDLL NTPVDHPSRR TSDSYYADKN
FVLRTHTTTM WPFYLKDPDV IEKLNETGCV KCLCHGKVFR KDEVDRKHFP VFHQIDGLYI
CDKKIKIIGI PELSEVLADI AKNIYGPDVE YQILEDSFPF TDPSIQIEIK KGDSWIEILG
AGVVHKKVLS NLGIDPEKYN GWAFGFGVER LAIAKMDIPD IRIFWSNDSR ITSQFKDINS
KYKEVSKFPA TDRDISFIID KSVNLNNYYE IVRDFAENLI EEVKLLDKYE DKEKFGEDKI
SYTFRITYRS IERTLTNEEI NKIQKKIRKK TERELSAKLR
//
