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Database: UniProt
Entry: N6X6W0_9ACTO
LinkDB: N6X6W0_9ACTO
Original site: N6X6W0_9ACTO 
ID   N6X6W0_9ACTO            Unreviewed;       361 AA.
AC   N6X6W0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00281};
DE            EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00281};
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00281};
DE            Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00281};
GN   Name=pheS {ECO:0000256|HAMAP-Rule:MF_00281,
GN   ECO:0000313|EMBL:ENO19092.1};
GN   ORFNames=HMPREF9004_0011 {ECO:0000313|EMBL:ENO19092.1};
OS   Schaalia cardiffensis F0333.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Schaalia.
OX   NCBI_TaxID=888050 {ECO:0000313|EMBL:ENO19092.1, ECO:0000313|Proteomes:UP000013015};
RN   [1] {ECO:0000313|EMBL:ENO19092.1, ECO:0000313|Proteomes:UP000013015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0333 {ECO:0000313|EMBL:ENO19092.1,
RC   ECO:0000313|Proteomes:UP000013015};
RA   Aqrawi P., Ayvaz T., Bess C., Blankenburg K., Coyle M., Deng J., Forbes L.,
RA   Fowler G., Francisco L., Fu Q., Gibbs R., Gross S., Gubbala S., Hale W.,
RA   Hemphill L., Highlander S., Hirani K., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jayaseelan J.C., Jiang H., Joshi V., Korchina V., Kovar C.,
RA   Lara F., Lee S., Liu Y., Mata R., Mathew T., Munidasa M., Muzny D.,
RA   Nazareth L., Ngo R., Nguyen L., Nguyen N., Okwuonu G., Ongeri F.,
RA   Palculict T., Patil S., Petrosino J., Pham C., Pham P., Pu L.-L., Qin X.,
RA   Qu J., Reid J., Ross M., Ruth R., Saada N., San Lucas F., Santibanez J.,
RA   Shang Y., Simmons D., Song X.-Z., Tang L.-Y., Thornton R., Warren J.,
RA   Weissenberger G., Wilczek-Boney K., Worley K., Youmans B., Zhang J.,
RA   Zhang L., Zhao Z., Zhou C., Zhu D., Zhu Y.;
RT   "Reference genome for the Human Microbiome Project.";
RL   Submitted (MAR-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, ECO:0000256|HAMAP-
CC         Rule:MF_00281};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00281};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_00281};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00281}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00281}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Phe-tRNA synthetase alpha subunit type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010207, ECO:0000256|HAMAP-Rule:MF_00281}.
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:ENO19092.1}.
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DR   EMBL; AQHZ01000001; ENO19092.1; -; Genomic_DNA.
DR   RefSeq; WP_005961495.1; NZ_KB822674.1.
DR   AlphaFoldDB; N6X6W0; -.
DR   STRING; 888050.HMPREF9004_0011; -.
DR   PATRIC; fig|888050.3.peg.11; -.
DR   eggNOG; COG0016; Bacteria.
DR   HOGENOM; CLU_025086_0_0_11; -.
DR   OrthoDB; 9800719at2; -.
DR   Proteomes; UP000013015; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00496; PheRS_alpha_core; 1.
DR   HAMAP; MF_00281; Phe_tRNA_synth_alpha1; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR   InterPro; IPR004188; Phe-tRNA_ligase_II_N.
DR   InterPro; IPR022911; Phe_tRNA_ligase_alpha1_bac.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   NCBIfam; TIGR00468; pheS; 1.
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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00281};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00281};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00281};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00281};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00281};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00281};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00281};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00281}; Reference proteome {ECO:0000313|Proteomes:UP000013015}.
FT   DOMAIN          124..333
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   BINDING         276
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with beta subunit"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00281"
SQ   SEQUENCE   361 AA;  39001 MW;  62039DCC32FF47E3 CRC64;
     MAQAALDLNP LDSEAVDDLV ARALADIEAA ADLEALKAVK SALLGDQAPL VLANRKIGQL
     APADRGTAGK NLGGARARLS QALTERGQIL EAEHEARVLV EESVDVTAFG ARSVIGARHP
     IGTLIEEIED FFTSMGWEIA EGPEIEHEWF NFDSLNFDID HPARQMQDTL YIDGTTIGGE
     APEDGCLVMR THTSPVQSRS LLARGVPLYV ACPGKVFRSD ALDATHTPVF HQVEGLAVDK
     GLTMAHLKGV LDHFAKAMFG PDAKARLRPS FFPFTEPSAE LDMWFPQKKG GAGWIEVGGC
     GMVNPNVLRA NGIDPDEYTG FAFGMGIERT LMLRHGIADM HDIVEGDVRF SQQFGLHGKG
     H
//
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