SYFB_DROME
ID SYFB_DROME Reviewed; 589 AA.
AC Q9VCA5;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit;
DE EC=6.1.1.20 {ECO:0000269|PubMed:25427601};
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
DE Short=PheRS;
GN Name=beta-PheRS {ECO:0000312|FlyBase:FBgn0039175};
GN ORFNames=CG5706 {ECO:0000312|FlyBase:FBgn0039175};
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-158.
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:A5K464};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Lethal. {ECO:0000269|PubMed:25427601}.
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit
CC family. Type 2 subfamily. {ECO:0000305}.
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DR EMBL; AE014297; AAF56268.1; -; Genomic_DNA.
DR EMBL; AY052086; AAK93510.1; -; mRNA.
DR RefSeq; NP_651237.1; NM_142980.4.
DR AlphaFoldDB; Q9VCA5; -.
DR SMR; Q9VCA5; -.
DR BioGRID; 67816; 2.
DR IntAct; Q9VCA5; 1.
DR STRING; 7227.FBpp0084021; -.
DR PaxDb; Q9VCA5; -.
DR PRIDE; Q9VCA5; -.
DR EnsemblMetazoa; FBtr0084637; FBpp0084021; FBgn0039175.
DR GeneID; 42888; -.
DR KEGG; dme:Dmel_CG5706; -.
DR UCSC; CG5706-RA; d. melanogaster.
DR CTD; 42888; -.
DR FlyBase; FBgn0039175; beta-PheRS.
DR VEuPathDB; VectorBase:FBgn0039175; -.
DR eggNOG; KOG2472; Eukaryota.
DR GeneTree; ENSGT00530000063489; -.
DR HOGENOM; CLU_020279_2_0_1; -.
DR InParanoid; Q9VCA5; -.
DR OMA; FPGRCAN; -.
DR OrthoDB; 378921at2759; -.
DR PhylomeDB; Q9VCA5; -.
DR BioGRID-ORCS; 42888; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42888; -.
DR PRO; PR:Q9VCA5; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039175; Expressed in eye disc (Drosophila) and 25 other tissues.
DR Genevisible; Q9VCA5; DM.
DR GO; GO:0005737; C:cytoplasm; TAS:FlyBase.
DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IBA:GO_Central.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IGI:FlyBase.
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; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IDA:FlyBase.
DR CDD; cd00769; PheRS_beta_core; 1.
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 Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..589
FT /note="Phenylalanine--tRNA ligase beta subunit"
FT /id="PRO_0000127019"
FT DOMAIN 302..377
FT /note="B5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00816"
FT BINDING 355
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 BINDING 364
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 365
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 MUTAGEN 158
FT /note="A->W: Reduced survival rate after 50 days of age.
FT Decreased aminoacylation, increased misacylation of non-
FT cognate Tyr, increased amino acid misincorporation,
FT ommatidia defects, neurodegeneration, impaired locomotive
FT performance, reduced lifespan, smaller organ size due to
FT apoptosis and increased ER stress; when associated with 'G-
FT 456' in alpha subunit."
FT /evidence="ECO:0000269|PubMed:25427601"
SQ SEQUENCE 589 AA; 65778 MW; D7596D94E97A4DA1 CRC64;
MPTIGVKRDL LFEALGKTYT DDEFQDLCFA FGLELDEVTT EKQMLTKEQG DVAAAANASE
EIIYRIDIPA NRYDLLCLEG LVTGLLVFQG KLKPPKFQFV ELAKRQVLKI DPSTAQIRPY
AVAAVLRNVT FTQASYNSFI DLQDKLHQNI CRKRTLVAIG THDLDTLQGP FSYEALAPDQ
IKFKPLNQTK EMTGSELMDF YSTHAQLKQY LPIIRESPVY PVIYDANRVV LSLPPIINGD
HSKITLKTKN VFIECTATDR TKAKVVLDTI VCLFSEHCAQ KFTVEPCDVV QPDGSVISYP
ELEVREERIS VKRANAYIGI DEPAEKLADM LTRMYLEAKV DGDSLVVKIP PTRHDVIHAC
DIYEDVAIAY GYNNIKKSLP AFMQIAKQFP LNKLTEQLRE QVAQAGFTEA LTFTLCSRDD
IGRKLNKNID ALPAVHIGNP KTLEFQVVRT TLLPGLLKTL VANRKMPLPL KLFEISDVVV
ADESTEVGAR NERRVCAVNC NKTAGFEVVH GLLDRVMQLL SVPWKSASGT KGYYLQATED
PSYFPGRCAN VMYDGVVIGK IGVLHPTVLQ AFELTTPCSA VEFTIEPFV
