GenomeNet

Database: UniProt
Entry: A0A1M6ILX4_9BACT
LinkDB: A0A1M6ILX4_9BACT
Original site: A0A1M6ILX4_9BACT 
ID   A0A1M6ILX4_9BACT        Unreviewed;       339 AA.
AC   A0A1M6ILX4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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   ORFNames=SAMN05444280_11743 {ECO:0000313|EMBL:SHJ35428.1};
OS   Tangfeifania diversioriginum.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC   Tangfeifania.
OX   NCBI_TaxID=1168035 {ECO:0000313|EMBL:SHJ35428.1, ECO:0000313|Proteomes:UP000184050};
RN   [1] {ECO:0000313|EMBL:SHJ35428.1, ECO:0000313|Proteomes:UP000184050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27063 {ECO:0000313|EMBL:SHJ35428.1,
RC   ECO:0000313|Proteomes:UP000184050};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FQZE01000017; SHJ35428.1; -; Genomic_DNA.
DR   RefSeq; WP_073169757.1; NZ_FQZE01000017.1.
DR   AlphaFoldDB; A0A1M6ILX4; -.
DR   STRING; 1168035.SAMN05444280_11743; -.
DR   OrthoDB; 9800719at2; -.
DR   Proteomes; UP000184050; 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:UP000184050}.
FT   DOMAIN          107..334
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   BINDING         250
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   339 AA;  38655 MW;  961FDCEEA9020BC8 CRC64;
     MLEKIKALQQ EIDEAKASTL EEVDELRIKY ISKKGKINQL FSDFKNVPNE QKKEVGKAIN
     DLKNFTLDKI NNLRDSFSKS DSGTDGLDLT RPGEPVKLGT RHPLALVKNE IINIFGRLGF
     AVAEGPEIED DWHVFSALNF PPEHPARDMQ DTFFIEKDPD ILLRTHTSSV QIRVMEQKEP
     PIRAIFPGRV FRNEAISARS HCIFHQVEGL YVDENVSFAD LKQTLLYFAK ELFGEETQIR
     LRPSYFPFTE PSAEMDVSCS ICGGEGCNVC KYTGWLEILG CGMVDPNVLE ACNIDSRKYT
     GFAFGMGIER IAMLRYGIKD IRYFFENDIR FLKQFESAI
//
DBGET integrated database retrieval system