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Database: UniProt
Entry: A0A0U3H6H9_9MICC
LinkDB: A0A0U3H6H9_9MICC
Original site: A0A0U3H6H9_9MICC 
ID   A0A0U3H6H9_9MICC        Unreviewed;       372 AA.
AC   A0A0U3H6H9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN   ORFNames=MB46_17440 {ECO:0000313|EMBL:ALV46998.1};
OS   Arthrobacter alpinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=656366 {ECO:0000313|EMBL:ALV46998.1, ECO:0000313|Proteomes:UP000055883};
RN   [1] {ECO:0000313|EMBL:ALV46998.1, ECO:0000313|Proteomes:UP000055883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A3 {ECO:0000313|EMBL:ALV46998.1,
RC   ECO:0000313|Proteomes:UP000055883};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226}.
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DR   EMBL; CP013745; ALV46998.1; -; Genomic_DNA.
DR   RefSeq; WP_044577404.1; NZ_CP013745.1.
DR   AlphaFoldDB; A0A0U3H6H9; -.
DR   KEGG; arw:MB46_17440; -.
DR   eggNOG; COG0016; Bacteria.
DR   OrthoDB; 489670at2; -.
DR   Proteomes; UP000055883; Chromosome.
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; 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; 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; PS51447; FDX_ACB; 1.
PE   3: Inferred from homology;
FT   DOMAIN          264..370
FT                   /note="FDX-ACB"
FT                   /evidence="ECO:0000259|PROSITE:PS51447"
SQ   SEQUENCE   372 AA;  39872 MW;  B066D9593D57B800 CRC64;
     MHTYLSHTAL QSALSVPDLS EAAAGHAMSA MLTSVTDALT TLWDVPVAEH RPSPLVSVRD
     NYDRLGFSPT DVTRDSRYSR HVSPTVMLRS HTSAGMPAVL DSLRPELGRY DTLHVLPGLV
     YRRDAVDRTH VGTPHQVDLW RLRSRGLLGV PDLTAMLGAV VEAVLPGARW RTISSPHPYT
     TAGVQLDVQV RGEWLELAEA GLVAATVLRA SGLDPRRWGG LALGMGLDRA LMLRKGIDDI
     RLLRSADPDV SAQMTDLSPY SAVSAMPPVH RDLSLVCADD VDPEVLGDAA RSALGPDAEV
     LAGVEVLAVT PVAKLPSGAV ARLGIVPGQA NVLVRLTLQS LERTLTSAEA NVVRNRVYKA
     LHEGPNLELI AV
//
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