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Database: UniProt
Entry: U7UQR4_9FIRM
LinkDB: U7UQR4_9FIRM
Original site: U7UQR4_9FIRM 
ID   U7UQR4_9FIRM            Unreviewed;       236 AA.
AC   U7UQR4;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN   ORFNames=HMPREF1250_2234 {ECO:0000313|EMBL:ERT61777.1};
OS   Megasphaera vaginalis.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=1111454 {ECO:0000313|EMBL:ERT61777.1, ECO:0000313|Proteomes:UP000017090};
RN   [1] {ECO:0000313|EMBL:ERT61777.1, ECO:0000313|Proteomes:UP000017090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BV3C16-1 {ECO:0000313|EMBL:ERT61777.1,
RC   ECO:0000313|Proteomes:UP000017090};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (SEP-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:ERT61777.1}.
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DR   EMBL; AWXA01000008; ERT61777.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7UQR4; -.
DR   STRING; 1111454.HMPREF1250_2234; -.
DR   PATRIC; fig|1111454.3.peg.572; -.
DR   eggNOG; COG0016; Bacteria.
DR   Proteomes; UP000017090; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0016740; F:transferase activity; IEA:UniProt.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004188; Phe-tRNA_ligase_II_N.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   PANTHER; PTHR11538:SF41; PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02912; Phe_tRNA-synt_N; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF46589; tRNA-binding arm; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   4: Predicted;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ERT61777.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017090}.
FT   DOMAIN          115..236
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   236 AA;  27257 MW;  E9980A39117F797D CRC64;
     MINEQIEAIK SAVAEQLAKT TTLQDVQDIR VRYLGKKGEL TSIMKELKTL SPEERPKVGQ
     LVNTARGLIE EELRKKTEEV KEKALAERLR SEKIDITLPG RRPVMGHEHP LHSTKRLMEK
     AFLQMGFSIV EGPEIEDDYY NFQCLNFPDD HPARDMQDSM YITDKILLRT HTSPMQARTL
     QAHRPNEPVK VIVPGKVYRW DYDATHSPVF HQMEGLIVDE NIRFSDLKGM LEVFFA
//
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