ID I1II18_BRADI Unreviewed; 594 AA.
AC I1II18;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN Name=100821229 {ECO:0000313|EnsemblPlants:KQJ86559};
GN ORFNames=BRADI_4g06310v3 {ECO:0000313|EMBL:KQJ86559.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ86559.1};
RN [1] {ECO:0000313|EMBL:KQJ86559.1, ECO:0000313|EnsemblPlants:KQJ86559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ86559.1,
RC ECO:0000313|EnsemblPlants:KQJ86559};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ86559.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ86559.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ86559}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ86559};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 2 subfamily. {ECO:0000256|ARBA:ARBA00007438}.
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DR EMBL; CM000883; KQJ86559.1; -; Genomic_DNA.
DR RefSeq; XP_003575955.1; XM_003575907.3.
DR AlphaFoldDB; I1II18; -.
DR STRING; 15368.I1II18; -.
DR EnsemblPlants; KQJ86559; KQJ86559; BRADI_4g06310v3.
DR GeneID; 100821229; -.
DR Gramene; KQJ86559; KQJ86559; BRADI_4g06310v3.
DR KEGG; bdi:100821229; -.
DR eggNOG; KOG2472; Eukaryota.
DR HOGENOM; CLU_020279_2_0_1; -.
DR InParanoid; I1II18; -.
DR OMA; FPGRCAN; -.
DR OrthoDB; 5473299at2759; -.
DR Proteomes; UP000008810; Chromosome 4.
DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00769; PheRS_beta_core; 1.
DR Gene3D; 3.30.56.10; -; 2.
DR Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005146; B3/B4_tRNA-bd.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR InterPro; IPR004531; Phe-tRNA-synth_IIc_bsu_arc_euk.
DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR InterPro; IPR041616; PheRS_beta_core.
DR InterPro; IPR040659; PhetRS_B1.
DR InterPro; IPR005147; tRNA_synthase_B5-dom.
DR NCBIfam; TIGR00471; pheT_arch; 1.
DR PANTHER; PTHR10947:SF0; PHENYLALANINE--TRNA LIGASE BETA SUBUNIT; 1.
DR PANTHER; PTHR10947; PHENYLALANYL-TRNA SYNTHETASE BETA CHAIN AND LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47; 1.
DR Pfam; PF03483; B3_4; 1.
DR Pfam; PF03484; B5; 1.
DR Pfam; PF18262; PhetRS_B1; 1.
DR Pfam; PF17759; tRNA_synthFbeta; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF56037; PheT/TilS domain; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 2.
DR PROSITE; PS51483; B5; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810}.
FT DOMAIN 305..384
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
SQ SEQUENCE 594 AA; 66767 MW; 924E31DCA7888F72 CRC64;
MPTVSVGRDR LFAALGRVYT QEEFEALCFE FGIELDDVTT EKAIIRKEKH LEEDGEADGE
DEVIYKIEVA ANRYDLLCLE GIARSLRIFI GAEATPLFKT SSIPRGSMLQ MHVRPQTAQI
RPYVVCAVLR GVTFDEVRYN SFIDLQDKLH QNICRKRTLV AIGTHDLDTL KGPFSYEALP
PQEINFVPLK QEQKFRADAL MDFYRSDMKL KKFLHIIENS PVYPVIYDSN RTVLSLPPII
NGAHSAITLK TRNVFIECTA TDLTKANIVL NTMVAMFSEY CENKFEVEPV EVVSSDGSKA
IYPDLSCYKL EVSLSDIVGP IGISLDETQV ISLLKKMQLQ AELCPSNGEP RFSVSVPPTR
SDILHARDLA EDVAIAYGYN NVPKSKPKSM TIGGRQPLNR FSDKIRAEVT RAGYMEVLTF
VLTSHEENFD MLNRTDDGNK AVIIANPRTS EFEVVRTSLM SCLLKTLKHN IDHPRPIKIF
EVGDVVALDA SRDVGASNNR RLAALYCNSN SGFEEIMGLV DRTVKIVRAP HINFGKTYYV
PTSEPEFFTK RQCKIVMSDG KQVGYLGIVH PEVLRKFGIP DPCTFVEIDI EALL
//
