ID A0A3Q7E8X9_SOLLC Unreviewed; 619 AA.
AC A0A3Q7E8X9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc01g008310.3.1};
RN [1] {ECO:0000313|EnsemblPlants:Solyc01g008310.3.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc01g008310.3.1};
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2] {ECO:0000313|EnsemblPlants:Solyc01g008310.3.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc01g008310.3.1};
RG EnsemblPlants;
RL Submitted (JAN-2019) 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 AlphaFoldDB; A0A3Q7E8X9; -.
DR STRING; 4081.A0A3Q7E8X9; -.
DR PaxDb; 4081-Solyc01g008310-2-1; -.
DR EnsemblPlants; Solyc01g008310.3.1; Solyc01g008310.3.1; Solyc01g008310.3.
DR Gramene; Solyc01g008310.3.1; Solyc01g008310.3.1; Solyc01g008310.3.
DR InParanoid; A0A3Q7E8X9; -.
DR OMA; FPGRCAN; -.
DR Proteomes; UP000004994; Chromosome 1.
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:UP000004994}.
FT DOMAIN 347..427
FT /note="B5"
FT /evidence="ECO:0000259|PROSITE:PS51483"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 619 AA; 69144 MW; 5C07F81D5C596C72 CRC64;
NYSPSSPTVP EPLPPSIFGS PVASDHRPPP LPPPPIFSDS GVTMPTVSVG RDRLFEALGR
TYTDEEFDEL CFQFGIELDD ITTEKAIQRK EKHLEEEGVE DDGETIYKIE VPANRYDLLC
LEGLAQALRI FNGLDPIPTY KVANIGKESM LEMRVKTETS KIRPYVVCAV LRGVTFDEAK
YNSFIELQDR LHQNICRRRT LVAIGTHDLD TIEGPFTYEA LPPAEINFVP LKQTKNFRAD
ELMEFYKSDL KLKKFLHIIE NSPVYPVIYD CKRTVLSLPP IINGAHSAIS LKTKNVFIEC
TATDLTKANI VLNTMVTMFS VYCERKFEVE PVKVTYPDGR SYVCPDLSIY NMNVPLSYIT
GIIGVQLPED KVASLLHKMQ LRAEKSVSED KEVKFVVSVP PTRSDVLHPC DVAEDVAIAY
GYNEIPKRKP ASLNPLPLSQ FSDLIRTEIA MTGYTEVLTW ILCSKKEIFS MLNREEDNSA
VTIADSRTSE FEVVRPSLMP GLLRTVGHNK DHPKPIKIFE VGDIVLLDDT KDVGAVNRRH
LAALYCGANS GFELIHGLVD KIMEATGTNF VSPGNSTGYY IEKSEEPAFL QGRQANVIYG
GKQIGTFGIV HPKFGPQGV
//
