SYFA_DROME
ID SYFA_DROME Reviewed; 498 AA.
AC Q9W3J5;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit;
DE EC=6.1.1.20 {ECO:0000269|PubMed:25427601};
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit;
DE Short=PheRS;
GN Name=alpha-PheRS {ECO:0000312|FlyBase:FBgn0030007};
GN ORFNames=CG2263 {ECO:0000312|FlyBase:FBgn0030007};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ALA-456.
RX PubMed=25427601; DOI=10.1038/ncomms6650;
RA Lu J., Bergert M., Walther A., Suter B.;
RT "Double-sieving-defective aminoacyl-tRNA synthetase causes protein
RT mistranslation and affects cellular physiology and development.";
RL Nat. Commun. 5:5650-5650(2014).
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:25427601};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A5K9S0};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Lethal when homozygous.
CC {ECO:0000269|PubMed:25427601}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Phe-tRNA synthetase alpha subunit type 2 subfamily. {ECO:0000305}.
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DR EMBL; AE014298; AAF46332.1; -; Genomic_DNA.
DR EMBL; AY051694; AAK93118.1; -; mRNA.
DR RefSeq; NP_572448.1; NM_132220.4.
DR AlphaFoldDB; Q9W3J5; -.
DR SMR; Q9W3J5; -.
DR BioGRID; 58208; 3.
DR STRING; 7227.FBpp0071138; -.
DR PaxDb; Q9W3J5; -.
DR PRIDE; Q9W3J5; -.
DR DNASU; 31740; -.
DR EnsemblMetazoa; FBtr0071190; FBpp0071138; FBgn0030007.
DR GeneID; 31740; -.
DR KEGG; dme:Dmel_CG2263; -.
DR UCSC; CG2263-RA; d. melanogaster.
DR CTD; 31740; -.
DR FlyBase; FBgn0030007; alpha-PheRS.
DR VEuPathDB; VectorBase:FBgn0030007; -.
DR eggNOG; KOG2784; Eukaryota.
DR GeneTree; ENSGT00390000006387; -.
DR HOGENOM; CLU_025086_2_2_1; -.
DR InParanoid; Q9W3J5; -.
DR OMA; QIEGWVM; -.
DR OrthoDB; 733355at2759; -.
DR PhylomeDB; Q9W3J5; -.
DR BioGRID-ORCS; 31740; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31740; -.
DR PRO; PR:Q9W3J5; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030007; Expressed in oviduct (Drosophila) and 37 other tissues.
DR Genevisible; Q9W3J5; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0004826; F:phenylalanine-tRNA ligase activity; IDA:FlyBase.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IDA:FlyBase.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR InterPro; IPR040724; PheRS_DBD1.
DR InterPro; IPR040586; PheRS_DBD2.
DR InterPro; IPR040725; PheRS_DBD3.
DR Pfam; PF18552; PheRS_DBD1; 1.
DR Pfam; PF18554; PheRS_DBD2; 1.
DR Pfam; PF18553; PheRS_DBD3; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00468; pheS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..498
FT /note="Phenylalanine--tRNA ligase alpha subunit"
FT /id="PRO_0000126825"
FT BINDING 328
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT BINDING 372..374
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT BINDING 412
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT BINDING 414
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="shared with beta subunit"
FT /evidence="ECO:0000250|UniProtKB:A5K9S0"
FT BINDING 438
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT MUTAGEN 456
FT /note="A->G: Decreased aminoacylation, increased
FT misacylation of non-cognate Tyr, increased amino acid
FT misincorporation, ommatidia defects, neurodegeneration,
FT impaired locomotive performance, reduced lifespan, smaller
FT organ size due to reduced cell proliferation and increased
FT ER stress. Similar but stronger phenotypes except that
FT smaller organ size is due primarily to apoptosis; when
FT associated with 'W-158' in beta subunit."
FT /evidence="ECO:0000269|PubMed:25427601"
SQ SEQUENCE 498 AA; 55684 MW; 496B5C1B2B07DEEC CRC64;
MHPDLTERIL QHLETTDKAD TLDLAALFAE DHQKIVGSLK SIQAHGELVT AETVTHKSLG
LTDEGRAVVE NGSHEALVYD LVPPEGIAQA ALMAAGGANA KVGFSKAMSH GWILVDKSVT
PPLVRRKVDT ITDVVRNQLQ QVALGKGDQL PAKEVADFKK RKLLQETTTK SFVLARGPEF
ATTLTKLETD LTVEMLANGL WDQLKFKAYN FDALGAPPTR GHLHPLLKVR TEFRQIFLEM
GFSEMPTNNY VESSFWNFDA LYQPQQHPAR DAHDTFFVNH PAKSHKFPQD YLERVKKVHS
VGGYGSKGYG YDWKLEEAQK NLLRTHTTAV SARMLYKLAN QEGGFKAAKY FSIDKVFRNE
TLDATHLAEF HQVEGVIADV GLTLGDLIGT LYEFFRKLGI TQLEFKPAYN PYTEPSMEIF
CYHPGLAKWI EVGNSGVFRP EMLLPMGLPE NVNVIAWGLS LERPTMIKYG INNIRDLVGP
KVDLKMVEEG PICRLDHA
