ID A0A1F5WYQ4_9BACT Unreviewed; 382 AA.
AC A0A1F5WYQ4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=A2930_01525 {ECO:0000313|EMBL:OGF80792.1};
OS Candidatus Giovannonibacteria bacterium RIFCSPLOWO2_01_FULL_45_34.
OC Bacteria; Candidatus Giovannonibacteria.
OX NCBI_TaxID=1798351 {ECO:0000313|EMBL:OGF80792.1, ECO:0000313|Proteomes:UP000178114};
RN [1] {ECO:0000313|EMBL:OGF80792.1, ECO:0000313|Proteomes:UP000178114}
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:OGF80792.1}.
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DR EMBL; MFID01000028; OGF80792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5WYQ4; -.
DR STRING; 1798351.A2930_01525; -.
DR Proteomes; UP000178114; 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 58..292
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT DOMAIN 288..382
FT /note="FDX-ACB"
FT /evidence="ECO:0000259|PROSITE:PS51447"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 44214 MW; B6F920718ABE6D72 CRC64;
MQDDRHIKID SPDSAKQRAE LEKRGDADAK RMLRFLDMPD LSRAEGSPLK ALIDLVLGIQ
DFKDFDAVEI PEIVPAKKSF DLFDFPAEHP ARSKSDTYYV NDEYILRTHT TVMWYYYLLS
ERAKAKLNGE EPVGIFSYGK VYRKDEIDRH HMNVFHQIDG LYLTWNDKRK IVKKDLEEVL
ANIAKAVFGP DIKYRFNDDS FPYTYDSIEM EVDKGGKWVE VLGAGIAQPS VLEKLGVDSK
IWGGWAFGFG LERLAIISME LPDIRLLWSE NARVKKQLKL GNKFKDVSKY PPITRDISFV
VNKDFIPNNY FDLIRDLGGD LVEQVELLDK YENAEKFGEG KISYAYRIIF RSNERTLITA
EADEIMKNIY GETEKQFNAE LR
//
