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Tyrosine--tRNA ligase (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (TyrRS)

 SYY_MIMIV               Reviewed;         346 AA.
Q5UPJ7;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
07-DEC-2004, sequence version 1.
28-MAR-2018, entry version 74.
RecName: Full=Tyrosine--tRNA ligase;
EC=6.1.1.1;
AltName: Full=Tyrosyl-tRNA synthetase;
Short=TyrRS;
Name=YARS; OrderedLocusNames=MIMI_L124;
Acanthamoeba polyphaga mimivirus (APMV).
Viruses; dsDNA viruses, no RNA stage; Mimiviridae; Mimivirus.
NCBI_TaxID=212035;
NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND FUNCTION.
STRAIN=Rowbotham-Bradford;
PubMed=15486256; DOI=10.1126/science.1101485;
Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
La Scola B., Susan M., Claverie J.-M.;
"The 1.2-megabase genome sequence of Mimivirus.";
Science 306:1344-1350(2004).
[2]
CRYSTALLIZATION, AND FUNCTION.
PubMed=16510997; DOI=10.1107/S174430910500062X;
Abergel C., Chenivesse S., Byrne D., Suhre K., Arondel V.,
Claverie J.-M.;
"Mimivirus TyrRS: preliminary structural and functional
characterization of the first amino-acyl tRNA synthetase found in a
virus.";
Acta Crystallogr. F 61:212-215(2005).
[3]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT, CATALYTIC ACTIVITY,
AND KINETIC PARAMETERS.
PubMed=17855524; DOI=10.1128/JVI.01107-07;
Abergel C., Rudinger-Thirion J., Giege R., Claverie J.-M.;
"Virus-encoded aminoacyl-tRNA synthetases: structural and functional
characterization of Mimivirus TyrRS and MetRS.";
J. Virol. 81:12406-12417(2007).
-!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a
two-step reaction: tyrosine is first activated by ATP to form Tyr-
AMP and then transferred to the acceptor end of tRNA(Tyr).
{ECO:0000250, ECO:0000269|PubMed:15486256,
ECO:0000269|PubMed:16510997}.
-!- CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP +
diphosphate + L-tyrosyl-tRNA(Tyr). {ECO:0000269|PubMed:17855524}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.5 uM for tRNA-Tyr {ECO:0000269|PubMed:17855524};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17855524}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-8356905, EBI-8356905;
-!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
family. {ECO:0000305}.
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EMBL; AY653733; AAV50399.1; -; Genomic_DNA.
RefSeq; YP_003986615.1; NC_014649.1.
PDB; 2J5B; X-ray; 2.20 A; A/B=2-346.
PDBsum; 2J5B; -.
DisProt; DP00726; -.
ProteinModelPortal; Q5UPJ7; -.
SMR; Q5UPJ7; -.
MINT; Q5UPJ7; -.
DrugBank; DB03978; Tyrosinal.
GeneID; 9924723; -.
KEGG; vg:9924723; -.
KO; K01866; -.
BRENDA; 6.1.1.1; 9231.
SABIO-RK; Q5UPJ7; -.
EvolutionaryTrace; Q5UPJ7; -.
Proteomes; UP000001134; Genome.
GO; GO:0005524; F:ATP binding; IDA:CAFA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
GO; GO:0072545; F:tyrosine binding; IDA:CAFA.
GO; GO:0004831; F:tyrosine-tRNA ligase activity; IDA:CAFA.
GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IDA:CAFA.
Gene3D; 3.40.50.620; -; 1.
InterPro; IPR002305; aa-tRNA-synth_Ic.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
InterPro; IPR023617; Tyr-tRNA-ligase_arc/euk-type.
Pfam; PF00579; tRNA-synt_1b; 1.
PIRSF; PIRSF006588; TyrRS_arch_euk; 1.
1: Evidence at protein level;
3D-structure; Aminoacyl-tRNA synthetase; ATP-binding;
Complete proteome; Ligase; Nucleotide-binding; Protein biosynthesis;
Reference proteome.
CHAIN 1 346 Tyrosine--tRNA ligase.
/FTId=PRO_0000055677.
MOTIF 47 56 "HIGH" region.
MOTIF 230 234 "KMSKS" region.
BINDING 233 233 ATP. {ECO:0000250}.
HELIX 6 17 {ECO:0000244|PDB:2J5B}.
STRAND 21 24 {ECO:0000244|PDB:2J5B}.
HELIX 26 35 {ECO:0000244|PDB:2J5B}.
STRAND 39 45 {ECO:0000244|PDB:2J5B}.
HELIX 53 68 {ECO:0000244|PDB:2J5B}.
STRAND 71 77 {ECO:0000244|PDB:2J5B}.
HELIX 79 84 {ECO:0000244|PDB:2J5B}.
HELIX 87 90 {ECO:0000244|PDB:2J5B}.
HELIX 92 108 {ECO:0000244|PDB:2J5B}.
HELIX 113 115 {ECO:0000244|PDB:2J5B}.
STRAND 116 120 {ECO:0000244|PDB:2J5B}.
HELIX 121 127 {ECO:0000244|PDB:2J5B}.
HELIX 129 147 {ECO:0000244|PDB:2J5B}.
HELIX 169 179 {ECO:0000244|PDB:2J5B}.
STRAND 186 188 {ECO:0000244|PDB:2J5B}.
HELIX 192 194 {ECO:0000244|PDB:2J5B}.
HELIX 195 207 {ECO:0000244|PDB:2J5B}.
STRAND 214 218 {ECO:0000244|PDB:2J5B}.
HELIX 236 238 {ECO:0000244|PDB:2J5B}.
HELIX 246 255 {ECO:0000244|PDB:2J5B}.
STRAND 260 262 {ECO:0000244|PDB:2J5B}.
HELIX 266 273 {ECO:0000244|PDB:2J5B}.
HELIX 275 279 {ECO:0000244|PDB:2J5B}.
STRAND 282 284 {ECO:0000244|PDB:2J5B}.
STRAND 287 291 {ECO:0000244|PDB:2J5B}.
HELIX 292 299 {ECO:0000244|PDB:2J5B}.
HELIX 304 325 {ECO:0000244|PDB:2J5B}.
HELIX 329 331 {ECO:0000244|PDB:2J5B}.
HELIX 332 340 {ECO:0000244|PDB:2J5B}.
SEQUENCE 346 AA; 39723 MW; 43C8D8C3ECBC87B0 CRC64;
MENTDHTNNE HRLTQLLSIA EECETLDRLK QLVDSGRIFT AYNGFEPSGR IHIAQALITV
MNTNNIIECG GQMIIYIADW FAKMNLKMNG DINKIRELGR YFIEVFKACG INLDGTRFIW
ASEFIASNPS YIERMLDIAE FSTISRVKRC CQIMGRNESD CLKASQIFYP CMQAADVFEL
VPEGIDICQL GIDQRKVNML AIEYANDRGL KIPISLSHHM LMSLSGPKKK MSKSDPQGAI
FMDDTEQEVS EKISRAYCTD ETFDNPIFEY IKYLLLRWFG TLNLCGKIYT DIESIQEDFS
SMNKRELKTD VANYINTIID LVREHFKKPE LSELLSNVKS YQQPSK


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