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Database: UniProt
Entry: A3YGG0_9GAMM
LinkDB: A3YGG0_9GAMM
Original site: A3YGG0_9GAMM 
ID   A3YGG0_9GAMM            Unreviewed;       321 AA.
AC   A3YGG0;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   13-SEP-2023, entry version 80.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|ARBA:ARBA00015409};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|ARBA:ARBA00030612};
DE   Flags: Fragment;
GN   ORFNames=MED121_03602 {ECO:0000313|EMBL:EAQ63751.1};
OS   Marinomonas sp. MED121.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=314277 {ECO:0000313|EMBL:EAQ63751.1, ECO:0000313|Proteomes:UP000003436};
RN   [1] {ECO:0000313|EMBL:EAQ63751.1, ECO:0000313|Proteomes:UP000003436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED121 {ECO:0000313|EMBL:EAQ63751.1,
RC   ECO:0000313|Proteomes:UP000003436};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (JAN-2006) 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|ARBA:ARBA00011209}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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}.
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:EAQ63751.1}.
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DR   EMBL; AANE01000018; EAQ63751.1; -; Genomic_DNA.
DR   RefSeq; WP_009836156.1; NZ_CH672435.1.
DR   AlphaFoldDB; A3YGG0; -.
DR   STRING; 314277.MED121_03602; -.
DR   HOGENOM; CLU_025086_0_1_6; -.
DR   OrthoDB; 9800719at2; -.
DR   Proteomes; UP000003436; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
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:0000313|EMBL:EAQ63751.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
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}.
FT   DOMAIN          106..311
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EAQ63751.1"
SQ   SEQUENCE   321 AA;  36426 MW;  DFBB53BFD31D2A79 CRC64;
     ALNAVSASDS ESALDEIRVR YLGKKGELTA LLKQLANVSA EDRPKFGQLV NEAKGQVQVE
     IAKRKEILAT QALNAKLATE TIDITLSGKG QEVGGLHPVT RTQERIENFF RGIGFDVAAG
     PEIEDDYHNF EALNIPEHHP ARAMQDTFYF NANTVLRTHT SPVQVRTMEK TQPPIRIVCP
     GRVYRCDSDQ THTPMFHQVE GLLIDENISF ADLKGVLQQF LNVFFEDDVK TRFRPSYFPF
     TEPSIEVDIW RINSKGEGSW LEVLGCGMVH PKVLEMSGID SEKYTGFAFG MGVERFAMLR
     YRVDDLRMFF ENDLRFLKQF K
//
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