SYY_MIMIV
ID SYY_MIMIV Reviewed; 346 AA.
AC Q5UPJ7;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Tyrosine--tRNA ligase;
DE EC=6.1.1.1;
DE AltName: Full=Tyrosyl-tRNA synthetase;
DE Short=TyrRS;
GN Name=YARS; OrderedLocusNames=MIMI_L124;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Mimivirus.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND FUNCTION.
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
RN [2]
RP CRYSTALLIZATION, AND FUNCTION.
RX PubMed=16510997; DOI=10.1107/s174430910500062x;
RA Abergel C., Chenivesse S., Byrne D., Suhre K., Arondel V., Claverie J.-M.;
RT "Mimivirus TyrRS: preliminary structural and functional characterization of
RT the first amino-acyl tRNA synthetase found in a virus.";
RL Acta Crystallogr. F 61:212-215(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT, CATALYTIC ACTIVITY, AND
RP KINETIC PARAMETERS.
RX PubMed=17855524; DOI=10.1128/jvi.01107-07;
RA Abergel C., Rudinger-Thirion J., Giege R., Claverie J.-M.;
RT "Virus-encoded aminoacyl-tRNA synthetases: structural and functional
RT characterization of Mimivirus TyrRS and MetRS.";
RL J. Virol. 81:12406-12417(2007).
CC -!- FUNCTION: Catalyzes the attachment of 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). {ECO:0000250,
CC ECO:0000269|PubMed:15486256, ECO:0000269|PubMed:16510997}.
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:0000269|PubMed:17855524};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 uM for tRNA-Tyr {ECO:0000269|PubMed:17855524};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17855524}.
CC -!- INTERACTION:
CC Q5UPJ7; Q5UPJ7: YARS; NbExp=3; IntAct=EBI-8356905, EBI-8356905;
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AY653733; AAV50399.1; -; Genomic_DNA.
DR RefSeq; YP_003986615.1; NC_014649.1.
DR PDB; 2J5B; X-ray; 2.20 A; A/B=2-346.
DR PDBsum; 2J5B; -.
DR SMR; Q5UPJ7; -.
DR MINT; Q5UPJ7; -.
DR DrugBank; DB03978; Tyrosinal.
DR GeneID; 9924723; -.
DR KEGG; vg:9924723; -.
DR BRENDA; 6.1.1.1; 9231.
DR SABIO-RK; Q5UPJ7; -.
DR EvolutionaryTrace; Q5UPJ7; -.
DR Proteomes; UP000001134; Genome.
DR GO; GO:0005524; F:ATP binding; IDA:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0072545; F:tyrosine binding; IDA:CAFA.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IDA:CAFA.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IDA:CAFA.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR023617; Tyr-tRNA-ligase_arc/euk-type.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR PIRSF; PIRSF006588; TyrRS_arch_euk; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..346
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000055677"
FT MOTIF 47..56
FT /note="'HIGH' region"
FT MOTIF 230..234
FT /note="'KMSKS' region"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:2J5B"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:2J5B"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 53..68
FT /evidence="ECO:0007829|PDB:2J5B"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 92..108
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2J5B"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 121..127
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 129..147
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:2J5B"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 195..207
FT /evidence="ECO:0007829|PDB:2J5B"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 246..255
FT /evidence="ECO:0007829|PDB:2J5B"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 275..279
FT /evidence="ECO:0007829|PDB:2J5B"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:2J5B"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 292..299
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 304..325
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:2J5B"
FT HELIX 332..340
FT /evidence="ECO:0007829|PDB:2J5B"
SQ 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
