SYY_ECOLI
ID SYY_ECOLI Reviewed; 424 AA.
AC P0AGJ9; P00951;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02006, ECO:0000305};
DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02006, ECO:0000269|PubMed:10572925, ECO:0000269|PubMed:11006270, ECO:0000269|PubMed:4292198, ECO:0000269|PubMed:4579631};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02006, ECO:0000303|PubMed:4579631};
DE Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02006, ECO:0000303|PubMed:10572925};
GN Name=tyrS {ECO:0000303|PubMed:6761148}; OrderedLocusNames=b1637, JW1629;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12;
RX PubMed=6761148; DOI=10.1016/0014-5793(82)80781-3;
RA Barker D.G., Bruton C.J., Winter G.;
RT "The tyrosyl-tRNA synthetase from Escherichia coli. Complete nucleotide
RT sequence of the structural gene.";
RL FEBS Lett. 150:419-423(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RC STRAIN=K12;
RX PubMed=1356963; DOI=10.1128/jb.174.19.6033-6045.1992;
RA Lam H.-M., Winkler M.E.;
RT "Characterization of the complex pdxH-tyrS operon of Escherichia coli K-12
RT and pleiotropic phenotypes caused by pdxH insertion mutations.";
RL J. Bacteriol. 174:6033-6045(1992).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBSTRATE SPECIFICITY.
RC STRAIN=B;
RX PubMed=4292198; DOI=10.1016/0022-2836(67)90259-8;
RA Calendar R., Berg P.;
RT "D-tyrosyl RNA: formation, hydrolysis and utilization for protein
RT synthesis.";
RL J. Mol. Biol. 26:39-54(1967).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=4579631; DOI=10.1016/0005-2787(73)90450-4;
RA Krajewska-Grynkiewicz K., Buonocore V., Schlesinger S.;
RT "Studies on the interaction of tyrosyl-tRNA synthetase from Escherichia
RT coli K12 with tyrosine and with tyrosyl-AMP.";
RL Biochim. Biophys. Acta 312:518-527(1973).
RN [8]
RP SUBUNIT.
RX PubMed=6754952; DOI=10.1016/0022-2836(82)90106-1;
RA Dessen P., Zaccai G., Blanquet S.;
RT "Neutron scattering studies of escherichia coli tyrosyl-trna synthetase and
RT of its interaction with trna tyr.";
RL J. Mol. Biol. 159:651-664(1982).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10572925; DOI=10.1016/s0304-4165(99)00103-8;
RA Airas R.K.;
RT "Chloride affects the interaction between tyrosyl-tRNA synthetase and
RT tRNA.";
RL Biochim. Biophys. Acta 1472:51-61(1999).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY,
RP AND MUTAGENESIS OF PHE-130.
RX PubMed=11006270; DOI=10.1074/jbc.m003696200;
RA Hamano-Takaku F., Iwama T., Saito-Yano S., Takaku K., Monden Y.,
RA Kitabatake M., Soll D., Nishimura S.;
RT "A mutant Escherichia coli tyrosyl-tRNA synthetase utilizes the unnatural
RT amino acid azatyrosine more efficiently than tyrosine.";
RL J. Biol. Chem. 275:40324-40328(2000).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-144, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [13]
RP ACETYLATION, AND ACTIVITY REGULATION.
RX PubMed=28741290; DOI=10.1002/cbic.201700343;
RA Venkat S., Gregory C., Gan Q., Fan C.;
RT "Biochemical characterization of the lysine acetylation of tyrosyl-tRNA
RT synthetase in Escherichia coli.";
RL ChemBioChem 18:1928-1934(2017).
RN [14] {ECO:0007744|PDB:1VBM, ECO:0007744|PDB:1X8X}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-322 IN COMPLEX WITH TYROSINE AND
RP TYR-AMP ANALOG, AND SUBUNIT.
RX PubMed=15663931; DOI=10.1016/j.jmb.2004.11.034;
RA Kobayashi T., Takimura T., Sekine R., Vincent K., Kamata K., Sakamoto K.,
RA Nishimura S., Yokoyama S.;
RT "Structural snapshots of the KMSKS loop rearrangement for amino acid
RT activation by bacterial tyrosyl-tRNA synthetase.";
RL J. Mol. Biol. 346:105-117(2005).
RN [15] {ECO:0007744|PDB:1VBN, ECO:0007744|PDB:1WQ3, ECO:0007744|PDB:1WQ4}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-322 OF MUTANT VAL-37/CYS-195 IN
RP COMPLEX WITH SUBSTRATE, AND SUBUNIT.
RX PubMed=15671170; DOI=10.1073/pnas.0407039102;
RA Kobayashi T., Sakamoto K., Takimura T., Sekine R., Kelly V.P., Kamata K.,
RA Nishimura S., Yokoyama S.;
RT "Structural basis of nonnatural amino acid recognition by an engineered
RT aminoacyl-tRNA synthetase for genetic code expansion.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1366-1371(2005).
RN [16] {ECO:0007744|PDB:2YXN}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-322 IN COMPLEX WITH
RP 3-AZIDO-L-TYROSINE.
RX PubMed=20159998; DOI=10.1093/nar/gkq080;
RA Iraha F., Oki K., Kobayashi T., Ohno S., Yokogawa T., Nishikawa K.,
RA Yokoyama S., Sakamoto K.;
RT "Functional replacement of the endogenous tyrosyl-tRNA synthetase-tRNATyr
RT pair by the archaeal tyrosine pair in Escherichia coli for genetic code
RT expansion.";
RL Nucleic Acids Res. 38:3682-3691(2010).
CC -!- FUNCTION: Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two-
CC step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC then transferred to the acceptor end of tRNA(Tyr) (PubMed:4292198,
CC PubMed:4579631). Can also mischarge tRNA(Tyr) with D-tyrosine, leading
CC to the formation of D-tyrosyl-tRNA(Tyr), which can be hydrolyzed by the
CC D-aminoacyl-tRNA deacylase (PubMed:4292198). In vitro, can also use the
CC non-natural amino acid azatyrosine (PubMed:11006270).
CC {ECO:0000269|PubMed:11006270, ECO:0000269|PubMed:4292198,
CC ECO:0000269|PubMed:4579631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-
CC tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02006,
CC ECO:0000269|PubMed:10572925, ECO:0000269|PubMed:11006270,
CC ECO:0000269|PubMed:4292198, ECO:0000269|PubMed:4579631};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-tyrosine + tRNA(Tyr) = AMP + D-tyrosyl-tRNA(Tyr) +
CC diphosphate + H(+); Xref=Rhea:RHEA:57448, Rhea:RHEA-COMP:9707,
CC Rhea:RHEA-COMP:9872, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58570, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78723, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:4292198};
CC -!- ACTIVITY REGULATION: Magnesium is essential for activity
CC (PubMed:4579631). Inhibited by chloride and sulfate in the presence of
CC 1 mM free Mg(2+). When the Mg(2+) concentration increases to 10 mM
CC there is almost no chloride inhibition any more. Inhibited by
CC diphosphate and AMP. Chloride strengthens the diphosphate inhibition
CC and weakens the AMP inhibition. Chloride weakens the binding of Mg(2+)
CC to the RNA and thereby the interaction between the enzyme and the RNA
CC (PubMed:10572925). Acetylation at certain lysine residues could
CC significantly impair activity (PubMed:28741290). D-tyrosine is a
CC competitive inhibitor of L-tyrosine for the formation of tyrosyl-
CC tRNA(Tyr) (PubMed:4292198). {ECO:0000269|PubMed:10572925,
CC ECO:0000269|PubMed:28741290, ECO:0000269|PubMed:4292198,
CC ECO:0000269|PubMed:4579631}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.027 mM for L-tyrosine {ECO:0000269|PubMed:4292198};
CC KM=0.0033 mM for L-tyrosine {ECO:0000269|PubMed:11006270};
CC KM=0.015 mM for D-tyrosine {ECO:0000269|PubMed:4292198};
CC KM=0.0177 mM for azatyrosine {ECO:0000269|PubMed:11006270};
CC KM=22 nM for tRNA(Tyr) (in the absence of KCl)
CC {ECO:0000269|PubMed:10572925};
CC KM=37 nM for tRNA(Tyr) (in the presence of 50 mM KCl)
CC {ECO:0000269|PubMed:10572925};
CC KM=93 nM for tRNA(Tyr) (in the presence of 100 mM KCl)
CC {ECO:0000269|PubMed:10572925};
CC KM=240 nM for tRNA(Tyr) (in the presence of 150 mM KCl)
CC {ECO:0000269|PubMed:10572925};
CC Vmax=2.6 umol/min/mg enzyme for L-tyrosine
CC {ECO:0000269|PubMed:4292198};
CC Vmax=0.11 umol/min/mg enzyme for D-tyrosine
CC {ECO:0000269|PubMed:4292198};
CC Note=kcat is 0.74 sec(-1) with L-tyrosine as substrate. kcat is 0.11
CC sec(-1) with azatyrosine as substrate. {ECO:0000269|PubMed:11006270};
CC -!- SUBUNIT: Homodimer (PubMed:4579631, PubMed:6754952, PubMed:15663931,
CC PubMed:15671170). Binds one molecule of tRNA(Tyr) per homodimer
CC (PubMed:6754952). {ECO:0000269|PubMed:15663931,
CC ECO:0000269|PubMed:15671170, ECO:0000269|PubMed:4579631,
CC ECO:0000269|PubMed:6754952}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02006,
CC ECO:0000305}.
CC -!- PTM: Acetylated at Lys-144 (PubMed:18723842, PubMed:28741290).
CC Acetylation at Lys-144 leads to slightly decreased activity
CC (PubMed:28741290). In vitro, in the presence of acetyl-phosphate, can
CC also be acetylated at Lys-67, Lys-85, Lys-90, Lys-230, Lys-235, Lys-
CC 238, Lys-321 and Lys-377. Acetylation at Lys-85, Lys-235 or Lys-238
CC causes dramatic decrease in activity (PubMed:28741290).
CC {ECO:0000269|PubMed:18723842, ECO:0000269|PubMed:28741290}.
CC -!- BIOTECHNOLOGY: Utilization for in vivo protein biosynthesis of mutants
CC that charge azatyrosine efficiently to tRNA may lead to efficient
CC production of azatyrosine-containing alloproteins, which have immense
CC potential in biotechnology and medicine. {ECO:0000269|PubMed:11006270}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02006, ECO:0000305}.
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DR EMBL; J01719; AAA24707.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74709.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15398.1; -; Genomic_DNA.
DR EMBL; M92351; AAA24710.1; -; Genomic_DNA.
DR PIR; A01178; SYECYT.
DR RefSeq; NP_416154.1; NC_000913.3.
DR RefSeq; WP_001295400.1; NZ_STEB01000003.1.
DR PDB; 1VBM; X-ray; 2.70 A; A/B=5-322.
DR PDB; 1VBN; X-ray; 2.70 A; A/B=5-322.
DR PDB; 1WQ3; X-ray; 2.00 A; A=1-322.
DR PDB; 1WQ4; X-ray; 2.00 A; A=2-322.
DR PDB; 1X8X; X-ray; 2.00 A; A=1-322.
DR PDB; 2YXN; X-ray; 1.80 A; A=1-322.
DR PDB; 6HB5; X-ray; 1.88 A; A/B=1-424.
DR PDB; 6HB6; X-ray; 1.92 A; A/B=1-424.
DR PDB; 6HB7; X-ray; 1.90 A; A/B=1-424.
DR PDB; 6I5Y; X-ray; 1.90 A; A/B=1-424.
DR PDB; 6WN2; X-ray; 1.78 A; A/B=1-322.
DR PDB; 7AP3; X-ray; 2.00 A; A/B=1-424.
DR PDBsum; 1VBM; -.
DR PDBsum; 1VBN; -.
DR PDBsum; 1WQ3; -.
DR PDBsum; 1WQ4; -.
DR PDBsum; 1X8X; -.
DR PDBsum; 2YXN; -.
DR PDBsum; 6HB5; -.
DR PDBsum; 6HB6; -.
DR PDBsum; 6HB7; -.
DR PDBsum; 6I5Y; -.
DR PDBsum; 6WN2; -.
DR PDBsum; 7AP3; -.
DR AlphaFoldDB; P0AGJ9; -.
DR SMR; P0AGJ9; -.
DR BioGRID; 4263487; 47.
DR DIP; DIP-36227N; -.
DR IntAct; P0AGJ9; 8.
DR STRING; 511145.b1637; -.
DR BindingDB; P0AGJ9; -.
DR ChEMBL; CHEMBL4295572; -.
DR DrugBank; DB01758; 3-Iodo-Tyrosine.
DR DrugBank; DB03325; Tyrosyladenylate.
DR iPTMnet; P0AGJ9; -.
DR SWISS-2DPAGE; P0AGJ9; -.
DR jPOST; P0AGJ9; -.
DR PaxDb; P0AGJ9; -.
DR PRIDE; P0AGJ9; -.
DR EnsemblBacteria; AAC74709; AAC74709; b1637.
DR EnsemblBacteria; BAA15398; BAA15398; BAA15398.
DR GeneID; 66674471; -.
DR GeneID; 948855; -.
DR KEGG; ecj:JW1629; -.
DR KEGG; eco:b1637; -.
DR PATRIC; fig|1411691.4.peg.623; -.
DR EchoBASE; EB1036; -.
DR eggNOG; COG0162; Bacteria.
DR InParanoid; P0AGJ9; -.
DR OMA; YMMAKDS; -.
DR PhylomeDB; P0AGJ9; -.
DR BioCyc; EcoCyc:TYRS-MON; -.
DR BioCyc; MetaCyc:TYRS-MON; -.
DR BRENDA; 6.1.1.1; 2026.
DR SABIO-RK; P0AGJ9; -.
DR EvolutionaryTrace; P0AGJ9; -.
DR PRO; PR:P0AGJ9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IDA:EcoCyc.
DR GO; GO:0043039; P:tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IDA:EcoCyc.
DR CDD; cd00165; S4; 1.
DR CDD; cd00805; TyrRS_core; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02006; Tyr_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR InterPro; IPR024107; Tyr-tRNA-ligase_bac_1.
DR PANTHER; PTHR11766; PTHR11766; 1.
DR Pfam; PF01479; S4; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
KW Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6761148"
FT CHAIN 2..424
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000055652"
FT DOMAIN 357..414
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT MOTIF 42..51
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT MOTIF 235..239
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 37
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006,
FT ECO:0000269|PubMed:15663931, ECO:0000305|PubMed:15671170"
FT BINDING 175
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006,
FT ECO:0000269|PubMed:15663931, ECO:0000269|PubMed:15671170,
FT ECO:0000305|PubMed:20159998"
FT BINDING 179
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006,
FT ECO:0000269|PubMed:15663931, ECO:0000269|PubMed:15671170,
FT ECO:0000305|PubMed:20159998"
FT BINDING 238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT SITE 231
FT /note="Cross-linked with tRNA by periodate oxidation"
FT SITE 235
FT /note="Cross-linked with tRNA by periodate oxidation;
FT predominant"
FT SITE 238
FT /note="Cross-linked with tRNA by periodate oxidation"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 37
FT /note="Y->V: Confers specificity for the non-natural amino
FT acid 3-iodo-tyrosine; when associated with C-195."
FT /evidence="ECO:0000269|PubMed:15671170"
FT MUTAGEN 130
FT /note="F->S: Utilizes the non-natural amino acid
FT azatyrosine more efficiently than tyrosine. Strong decrease
FT in affinity for tyrosine and small increase in affinity for
FT azatyrosine. Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:11006270"
FT MUTAGEN 195
FT /note="Q->C: Confers specificity for the non-natural amino
FT acid 3-iodo-tyrosine; when associated with V-37."
FT /evidence="ECO:0000269|PubMed:15671170"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:6WN2"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:6WN2"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:6WN2"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:6WN2"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 94..108
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6WN2"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:2YXN"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6WN2"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 175..190
FT /evidence="ECO:0007829|PDB:6WN2"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 202..216
FT /evidence="ECO:0007829|PDB:6WN2"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:6WN2"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1VBM"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:6WN2"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 265..275
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 280..291
FT /evidence="ECO:0007829|PDB:6WN2"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 299..320
FT /evidence="ECO:0007829|PDB:6WN2"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:7AP3"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:6HB5"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:6HB5"
FT HELIX 359..365
FT /evidence="ECO:0007829|PDB:6HB5"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:6HB5"
FT HELIX 372..380
FT /evidence="ECO:0007829|PDB:6HB5"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:6HB5"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:6HB5"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:6HB5"
FT STRAND 408..413
FT /evidence="ECO:0007829|PDB:6HB5"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:6HB5"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:6HB5"
SQ SEQUENCE 424 AA; 47527 MW; 98E7080D85B356A2 CRC64;
MASSNLIKQL QERGLVAQVT DEEALAERLA QGPIALYCGF DPTADSLHLG HLVPLLCLKR
FQQAGHKPVA LVGGATGLIG DPSFKAAERK LNTEETVQEW VDKIRKQVAP FLDFDCGENS
AIAANNYDWF GNMNVLTFLR DIGKHFSVNQ MINKEAVKQR LNREDQGISF TEFSYNLLQG
YDFACLNKQY GVVLQIGGSD QWGNITSGID LTRRLHQNQV FGLTVPLITK ADGTKFGKTE
GGAVWLDPKK TSPYKFYQFW INTADADVYR FLKFFTFMSI EEINALEEED KNSGKAPRAQ
YVLAEQVTRL VHGEEGLQAA KRITECLFSG SLSALSEADF EQLAQDGVPM VEMEKGADLM
QALVDSELQP SRGQARKTIA SNAITINGEK QSDPEYFFKE EDRLFGRFTL LRRGKKNYCL
ICWK
