SYFB_PLAVS
ID SYFB_PLAVS Reviewed; 617 AA.
AC A5K464;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit {ECO:0000305};
DE EC=6.1.1.20 {ECO:0000269|PubMed:33436639};
DE AltName: Full=Phenylalanine tRNA-synthetase beta subunit {ECO:0000303|PubMed:33436639};
DE Short=FRS {ECO:0000303|PubMed:33436639};
DE Short=PheRS {ECO:0000303|PubMed:33436639};
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit {ECO:0000305};
GN ORFNames=PVX_090880 {ECO:0000312|EMBL:EDL45442.1};
OS Plasmodium vivax (strain Salvador I).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=126793 {ECO:0000312|Proteomes:UP000008333};
RN [1] {ECO:0000312|EMBL:EDL45442.1, ECO:0000312|Proteomes:UP000008333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Salvador I {ECO:0000312|EMBL:EDL45442.1,
RC ECO:0000312|Proteomes:UP000008333};
RX PubMed=18843361; DOI=10.1038/nature07327;
RA Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., Caler E.,
RA Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., Cheng Q.,
RA Coulson R.M.R., Crabb B.S., del Portillo H.A., Essien K., Feldblyum T.V.,
RA Fernandez-Becerra C., Gilson P.R., Gueye A.H., Guo X., Kang'a S.,
RA Kooij T.W.A., Korsinczky M., Meyer E.V.-S., Nene V., Paulsen I., White O.,
RA Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., Stoeckert C.J.,
RA Sullivan S.A., Yamamoto M.M., Hoffman S.L., Wortman J.R., Gardner M.J.,
RA Galinski M.R., Barnwell J.W., Fraser-Liggett C.M.;
RT "Comparative genomics of the neglected human malaria parasite Plasmodium
RT vivax.";
RL Nature 455:757-763(2008).
RN [2] {ECO:0007744|PDB:7BY6}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 2-617 IN COMPLEX WITH ALPHA
RP SUBUNIT AND MAGNESIUM, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP AND SUBUNIT.
RX PubMed=33436639; DOI=10.1038/s41467-020-20478-5;
RA Sharma M., Malhotra N., Yogavel M., Harlos K., Melillo B., Comer E.,
RA Gonse A., Parvez S., Mitasev B., Fang F.G., Schreiber S.L., Sharma A.;
RT "Structural basis of malaria parasite phenylalanine tRNA-synthetase
RT inhibition by bicyclic azetidines.";
RL Nat. Commun. 12:343-343(2021).
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:0000269|PubMed:33436639};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:33436639};
CC -!- ACTIVITY REGULATION: Inhibited by bicyclic azetidine BRD1389, which
CC competes for L-phenylalanine. {ECO:0000269|PubMed:33436639}.
CC -!- SUBUNIT: Heterotetramer; dimer of two heterodimers formed by alpha and
CC beta subunits. {ECO:0000269|PubMed:33436639}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9NSD9}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 2 subfamily. {ECO:0000305}.
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DR EMBL; AAKM01000005; EDL45442.1; -; Genomic_DNA.
DR RefSeq; XP_001615169.1; XM_001615119.1.
DR PDB; 7BY6; X-ray; 3.00 A; B=2-617.
DR PDBsum; 7BY6; -.
DR SMR; A5K464; -.
DR STRING; 126793.A5K464; -.
DR EnsemblProtists; EDL45442; EDL45442; PVX_090880.
DR GeneID; 5474465; -.
DR KEGG; pvx:PVX_090880; -.
DR VEuPathDB; PlasmoDB:PVX_090880; -.
DR InParanoid; A5K464; -.
DR OMA; FPGRCAN; -.
DR PhylomeDB; A5K464; -.
DR Proteomes; UP000008333; Chromosome 9.
DR Proteomes; UP000008333; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IC:UniProtKB.
DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IC:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IDA:UniProtKB.
DR GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.50.40.10; -; 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 PANTHER; PTHR10947; PTHR10947; 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; SSF46955; SSF46955; 2.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00471; pheT_arch; 1.
DR PROSITE; PS51483; B5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..617
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000456102"
FT DOMAIN 297..374
FT /note="B5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT BINDING 358
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816,
FT ECO:0000269|PubMed:33436639, ECO:0007744|PDB:7BY6"
FT BINDING 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with alpha subunit"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
SQ SEQUENCE 617 AA; 71384 MW; B5FF4793F2D6CA39 CRC64;
MPTISVHEED LIEKLGEKIE EEKLNDICFE FGIEIDDVEY KGEKKIYKIE VPANRYDLVC
VEGLCRALKS FIGKYENVSY ALLTNSEEAC VKEKHFMRVD ESVDERRSYV VSAVLKNVKM
NENVYNNIIE LQEKLHHNLG KKRILLAIGI HDYDKINFPV AYKFEEKEKI NFIPLNETQN
VNGNNFINFY QDNINLKSYL KIISDFEKFP VIVDAGGQIL SLPPIINCDY TKITYDTRNL
FIECTAIDRN KAEIAVNIIC SMLSEYCTPK YSIHSFFVQY DKNHKAEKGN GYLYPVFKNK
TLTCHMDYVR KLSGILNLSV KDVEPLLKKM MITSKVIDSS TFTVDVPFYR SDIMHFCDIV
EDIAIAYGYG NIVSEKIEIA KKNSLSACTE LFRNVLAECT YTEVMTNALL SKRENYDCML
RKHRSYDDRK INLDEYNPLA PPVQIMNSKT SEYEIVRTSL IVNMLKFVSA NKHRELPLRF
FEIGDVSYTT YDRTDTNAVN KRYLSVIFAD KFTAGLEEAH GMLETVLKEF QLFSDYKIEE
KSKENVAIRS DVFYKLVPKE DPSFLNERVV DIVLCPHNLK FGIMGIIHPK VLENFSIDIP
VSVIEINIET IMDVLMM
