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Entry: K7KNG2_SOYBN
LinkDB: K7KNG2_SOYBN
Original site: K7KNG2_SOYBN 
ID   K7KNG2_SOYBN            Unreviewed;       630 AA.
AC   K7KNG2;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=phenylalanine--tRNA ligase {ECO:0000256|ARBA:ARBA00012814};
DE            EC=6.1.1.20 {ECO:0000256|ARBA:ARBA00012814};
GN   Name=100805249 {ECO:0000313|EnsemblPlants:KRH56733};
GN   ORFNames=GLYMA_05G016400 {ECO:0000313|EMBL:KRH56732.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH56733};
RN   [1] {ECO:0000313|EMBL:KRH56732.1, ECO:0000313|EnsemblPlants:KRH56733}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH56733};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH56732.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH56733}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH56733};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH56732.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH56732.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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; CM000838; KRH56732.1; -; Genomic_DNA.
DR   EMBL; CM000838; KRH56733.1; -; Genomic_DNA.
DR   RefSeq; XP_003524503.2; XM_003524455.3.
DR   AlphaFoldDB; K7KNG2; -.
DR   SMR; K7KNG2; -.
DR   STRING; 3847.K7KNG2; -.
DR   PaxDb; 3847-GLYMA05G07640-3; -.
DR   EnsemblPlants; KRH56732; KRH56732; GLYMA_05G016400.
DR   EnsemblPlants; KRH56733; KRH56733; GLYMA_05G016400.
DR   GeneID; 100805249; -.
DR   Gramene; KRH56732; KRH56732; GLYMA_05G016400.
DR   Gramene; KRH56733; KRH56733; GLYMA_05G016400.
DR   KEGG; gmx:100805249; -.
DR   eggNOG; KOG2472; Eukaryota.
DR   HOGENOM; CLU_020279_2_0_1; -.
DR   InParanoid; K7KNG2; -.
DR   OMA; FPGRCAN; -.
DR   OrthoDB; 5473299at2759; -.
DR   Proteomes; UP000008827; Chromosome 5.
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:UP000008827}.
FT   DOMAIN          331..411
FT                   /note="B5"
FT                   /evidence="ECO:0000259|PROSITE:PS51483"
SQ   SEQUENCE   630 AA;  70783 MW;  CAC8E125E44690C7 CRC64;
     MYPSDSEHLF LRRGCTCTHS IRDQNGAMPT VSVGRDRLFA ALGKTYTQEE FEDLCFSFGI
     ELDDVTTEKA IVRKEKHLEE EEADEDEEVI YKIEVPANRY DLLCLEGLAQ ALRVFCEFQE
     IPTYKLSKIS KDAMLKMHVK PETSLIRPYV VCAVLRGITF DKARYNSFID LQDKLHQNIC
     RRRTLVAIGT HDLDTLEGPF TYEALPPSSI TFTPLKQERN FRADDLMEFY KSDLKLKKFL
     HIIEDSPVFP VIYDSKRTVL SLPPIINGAH SAITLETKNV FIECTATDLT KAKVVLNTMV
     TAFSEYCENK FVIEPVEVIS SDGKSNIYPD LSVYNMEVSL SYITGLIGVS LEAEEVTKFL
     NRMQLHAKLS TSDNKQCNFV VSVPPSRSDV LHPCDVMEDV AIAYGFNAIK DQAVVDNKGS
     KRLAASLTLL PLNELSDLIR KEVALIGFTE VLTFILCSKK ENFAMLNRND DKSKAVIIGN
     PRSSDFEAVR TSLMPGILKT VAHNKDHPKP IKIFEVGDIA VLDDKRDVGA KNLRQLAALY
     CGANAGFEII HGLVDRVMEK NGVPFVSPGD KSGYYIEQSD EPEFLAGRQA RIIYKGKHIG
     TFGIVHPEVL NNFDIPDPCS FVELNIESFL
//
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