SYFA_HUMAN
ID SYFA_HUMAN Reviewed; 508 AA.
AC Q9Y285; B4E363; Q9NSD8; Q9Y4W8;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit;
DE EC=6.1.1.20 {ECO:0000269|PubMed:20223217};
DE AltName: Full=CML33;
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit;
DE Short=PheRS;
GN Name=FARSA; Synonyms=FARS, FARSL, FARSLA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9177188; DOI=10.1073/pnas.94.12.6164;
RA Sen S., Zhou H., Ripmaster T., Hittelman W.N., Schimmel P., White R.A.;
RT "Expression of a gene encoding a tRNA synthetase-like protein is enhanced
RT in tumorigenic human myeloid leukemia cells and is cell cycle stage- and
RT differentiation-dependent.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6164-6169(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10049785; DOI=10.1006/bbrc.1999.0141;
RA Rodova M., Ankilova V., Safro M.G.;
RT "Human phenylalanyl-tRNA synthetase: cloning, characterization of the
RT deduced amino acid sequences in terms of the structural domains and
RT coordinately regulated expression of the alpha and beta subunits in chronic
RT myeloid leukemia cells.";
RL Biochem. Biophys. Res. Commun. 255:765-773(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Motegi H., Noda T., Shiba K.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Leukocyte, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-12.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP PROTEIN SEQUENCE OF 2-12 AND 326-334, ACETYLATION AT ALA-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-311, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-190, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [18]
RP INVOLVEMENT IN RILDBC2, AND VARIANTS RILDBC2 LEU-256 AND LYS-410.
RX PubMed=31355908; DOI=10.1111/cge.13614;
RA Krenke K., Szczaluba K., Bielecka T., Rydzanicz M., Lange J., Koppolu A.,
RA Ploski R.;
RT "FARSA mutations mimic phenylalanyl-tRNA synthetase deficiency caused by
RT FARSB defects.";
RL Clin. Genet. 96:468-472(2019).
RN [19] {ECO:0007744|PDB:3L4G}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) IN COMPLEX WITH L-PHENYLALANINE,
RP CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=20223217; DOI=10.1016/j.str.2010.01.002;
RA Finarov I., Moor N., Kessler N., Klipcan L., Safro M.G.;
RT "Structure of human cytosolic phenylalanyl-tRNA synthetase: evidence for
RT kingdom-specific design of the active sites and tRNA binding patterns.";
RL Structure 18:343-353(2010).
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:20223217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19414;
CC Evidence={ECO:0000305|PubMed:20223217};
CC -!- SUBUNIT: Heterotetramer; dimer of two heterodimers formed by FARSA and
CC FARSB. {ECO:0000269|PubMed:20223217}.
CC -!- INTERACTION:
CC Q9Y285; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-725361, EBI-742038;
CC Q9Y285; Q9H9E3: COG4; NbExp=3; IntAct=EBI-725361, EBI-368382;
CC Q9Y285; Q9BQ95: ECSIT; NbExp=2; IntAct=EBI-725361, EBI-712452;
CC Q9Y285; Q9NSD9: FARSB; NbExp=7; IntAct=EBI-725361, EBI-353803;
CC Q9Y285; Q9BUL8: PDCD10; NbExp=3; IntAct=EBI-725361, EBI-740195;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q505J8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y285-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y285-2; Sequence=VSP_056196;
CC -!- DISEASE: Rajab interstitial lung disease with brain calcifications 2
CC (RILDBC2) [MIM:619013]: An autosomal recessive disorder characterized
CC by interstitial lung disease, growth delay, hypotonia, liver disease,
CC and brain abnormalities including diffuse, symmetrical brain
CC calcifications and periventricular cysts.
CC {ECO:0000269|PubMed:31355908}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Phe-tRNA synthetase alpha subunit type 2 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51175.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U07424; AAB61694.1; -; mRNA.
DR EMBL; AF042347; AAD02221.1; -; mRNA.
DR EMBL; D84471; BAA95666.1; -; mRNA.
DR EMBL; BT007198; AAP35862.1; -; mRNA.
DR EMBL; AK304587; BAG65375.1; -; mRNA.
DR EMBL; AD000092; AAB51175.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC006495; AAH06495.1; -; mRNA.
DR EMBL; BC043565; AAH43565.1; -; mRNA.
DR CCDS; CCDS12287.1; -. [Q9Y285-1]
DR PIR; T45074; T45074.
DR RefSeq; NP_004452.1; NM_004461.2. [Q9Y285-1]
DR PDB; 3L4G; X-ray; 3.30 A; A/C/E/G/I/K/M/O=1-508.
DR PDBsum; 3L4G; -.
DR AlphaFoldDB; Q9Y285; -.
DR SMR; Q9Y285; -.
DR BioGRID; 108487; 128.
DR ComplexPortal; CPX-2208; Phenylalanyl-tRNA synthetase complex.
DR DIP; DIP-53610N; -.
DR IntAct; Q9Y285; 54.
DR MINT; Q9Y285; -.
DR STRING; 9606.ENSP00000320309; -.
DR DrugBank; DB00120; Phenylalanine.
DR GlyGen; Q9Y285; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y285; -.
DR MetOSite; Q9Y285; -.
DR PhosphoSitePlus; Q9Y285; -.
DR SwissPalm; Q9Y285; -.
DR BioMuta; FARSA; -.
DR DMDM; 12643946; -.
DR EPD; Q9Y285; -.
DR jPOST; Q9Y285; -.
DR MassIVE; Q9Y285; -.
DR MaxQB; Q9Y285; -.
DR PaxDb; Q9Y285; -.
DR PeptideAtlas; Q9Y285; -.
DR PRIDE; Q9Y285; -.
DR ProteomicsDB; 5881; -.
DR ProteomicsDB; 85694; -. [Q9Y285-1]
DR Antibodypedia; 1072; 142 antibodies from 24 providers.
DR DNASU; 2193; -.
DR Ensembl; ENST00000314606.9; ENSP00000320309.3; ENSG00000179115.11. [Q9Y285-1]
DR Ensembl; ENST00000423140.6; ENSP00000396548.2; ENSG00000179115.11. [Q9Y285-2]
DR GeneID; 2193; -.
DR KEGG; hsa:2193; -.
DR MANE-Select; ENST00000314606.9; ENSP00000320309.3; NM_004461.3; NP_004452.1.
DR UCSC; uc002mvs.3; human. [Q9Y285-1]
DR CTD; 2193; -.
DR DisGeNET; 2193; -.
DR GeneCards; FARSA; -.
DR HGNC; HGNC:3592; FARSA.
DR HPA; ENSG00000179115; Low tissue specificity.
DR MalaCards; FARSA; -.
DR MIM; 602918; gene.
DR MIM; 619013; phenotype.
DR neXtProt; NX_Q9Y285; -.
DR OpenTargets; ENSG00000179115; -.
DR PharmGKB; PA28005; -.
DR VEuPathDB; HostDB:ENSG00000179115; -.
DR eggNOG; KOG2784; Eukaryota.
DR GeneTree; ENSGT00390000006387; -.
DR HOGENOM; CLU_025086_2_2_1; -.
DR InParanoid; Q9Y285; -.
DR OMA; QIEGWVM; -.
DR OrthoDB; 733355at2759; -.
DR PhylomeDB; Q9Y285; -.
DR TreeFam; TF300647; -.
DR BRENDA; 6.1.1.20; 2681.
DR PathwayCommons; Q9Y285; -.
DR Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation.
DR SignaLink; Q9Y285; -.
DR BioGRID-ORCS; 2193; 784 hits in 1090 CRISPR screens.
DR ChiTaRS; FARSA; human.
DR GeneWiki; FARSA_(gene); -.
DR GenomeRNAi; 2193; -.
DR Pharos; Q9Y285; Tbio.
DR PRO; PR:Q9Y285; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9Y285; protein.
DR Bgee; ENSG00000179115; Expressed in prefrontal cortex and 192 other tissues.
DR ExpressionAtlas; Q9Y285; baseline and differential.
DR Genevisible; Q9Y285; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000049; F:tRNA 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 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 InterPro; IPR036390; WH_DNA-bd_sf.
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; SSF46785; SSF46785; 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 3D-structure; Acetylation; Alternative splicing; Aminoacyl-tRNA synthetase;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Disease variant; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.9,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..508
FT /note="Phenylalanine--tRNA ligase alpha subunit"
FT /id="PRO_0000126824"
FT BINDING 329
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000269|PubMed:20223217,
FT ECO:0007744|PDB:3L4G"
FT BINDING 372..374
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000269|PubMed:20223217,
FT ECO:0007744|PDB:3L4G"
FT BINDING 412
FT /ligand="L-phenylalanine"
FT /ligand_id="ChEBI:CHEBI:58095"
FT /evidence="ECO:0000269|PubMed:20223217,
FT ECO:0007744|PDB:3L4G"
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:0000269|PubMed:20223217,
FT ECO:0007744|PDB:3L4G"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 190
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0C7"
FT MOD_RES 311
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 169..199
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056196"
FT VARIANT 256
FT /note="F -> L (in RILDBC2; unknown pathological
FT significance; dbSNP:rs941586004)"
FT /evidence="ECO:0000269|PubMed:31355908"
FT /id="VAR_084994"
FT VARIANT 341
FT /note="Q -> R (in dbSNP:rs35087277)"
FT /id="VAR_052641"
FT VARIANT 410
FT /note="N -> K (in RILDBC2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31355908"
FT /id="VAR_084995"
FT CONFLICT 179
FT /note="S -> G (in Ref. 3; BAA95666)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="V -> L (in Ref. 3; BAA95666)"
FT /evidence="ECO:0000305"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:3L4G"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:3L4G"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:3L4G"
FT TURN 144..149
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 153..161
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:3L4G"
FT TURN 194..198
FT /evidence="ECO:0007829|PDB:3L4G"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 226..240
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:3L4G"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 290..301
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 329..340
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 348..357
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 368..381
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 384..396
FT /evidence="ECO:0007829|PDB:3L4G"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 414..421
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 430..436
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:3L4G"
FT STRAND 452..461
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 462..465
FT /evidence="ECO:0007829|PDB:3L4G"
FT TURN 466..470
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:3L4G"
FT HELIX 484..489
FT /evidence="ECO:0007829|PDB:3L4G"
FT TURN 497..499
FT /evidence="ECO:0007829|PDB:3L4G"
SQ SEQUENCE 508 AA; 57564 MW; 99BC12E1F3C5FCFD CRC64;
MADGQVAELL LRRLEASDGG LDSAELAAEL GMEHQAVVGA VKSLQALGEV IEAELRSTKH
WELTAEGEEI AREGSHEARV FRSIPPEGLA QSELMRLPSG KVGFSKAMSN KWIRVDKSAA
DGPRVFRVVD SMEDEVQRRL QLVRGGQAEK LGEKERSELR KRKLLAEVTL KTYWVSKGSA
FSTSISKQET ELSPEMISSG SWRDRPFKPY NFLAHGVLPD SGHLHPLLKV RSQFRQIFLE
MGFTEMPTDN FIESSFWNFD ALFQPQQHPA RDQHDTFFLR DPAEALQLPM DYVQRVKRTH
SQGGYGSQGY KYNWKLDEAR KNLLRTHTTS ASARALYRLA QKKPFTPVKY FSIDRVFRNE
TLDATHLAEF HQIEGVVADH GLTLGHLMGV LREFFTKLGI TQLRFKPAYN PYTEPSMEVF
SYHQGLKKWV EVGNSGVFRP EMLLPMGLPE NVSVIAWGLS LERPTMIKYG INNIRELVGH
KVNLQMVYDS PLCRLDAEPR PPPTQEAA
