SYY_MYCPU
ID SYY_MYCPU Reviewed; 414 AA.
AC Q98Q81;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Tyrosine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02006};
DE EC=6.1.1.1 {ECO:0000255|HAMAP-Rule:MF_02006};
DE AltName: Full=Tyrosyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02006};
DE Short=TyrRS {ECO:0000255|HAMAP-Rule:MF_02006};
GN Name=tyrS {ECO:0000255|HAMAP-Rule:MF_02006}; OrderedLocusNames=MYPU_4850;
OS Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=272635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAB CTIP;
RX PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT pulmonis.";
RL Nucleic Acids Res. 29:2145-2153(2001).
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:0000255|HAMAP-
CC Rule:MF_02006}.
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 -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02006}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC TyrS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02006}.
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DR EMBL; AL445564; CAC13658.1; -; Genomic_DNA.
DR PIR; E90572; E90572.
DR RefSeq; WP_010925286.1; NC_002771.1.
DR AlphaFoldDB; Q98Q81; -.
DR SMR; Q98Q81; -.
DR STRING; 272635.MYPU_4850; -.
DR EnsemblBacteria; CAC13658; CAC13658; CAC13658.
DR KEGG; mpu:MYPU_4850; -.
DR eggNOG; COG0162; Bacteria.
DR HOGENOM; CLU_024003_0_2_14; -.
DR OMA; YMMAKDS; -.
DR OrthoDB; 402899at2; -.
DR BioCyc; MPUL272635:G1GT6-489-MON; -.
DR Proteomes; UP000000528; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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; PF00579; tRNA-synt_1b; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR TIGRFAMs; TIGR00234; tyrS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..414
FT /note="Tyrosine--tRNA ligase"
FT /id="PRO_0000234737"
FT DOMAIN 349..413
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT MOTIF 43..52
FT /note="'HIGH' region"
FT MOTIF 227..231
FT /note="'KMSKS' region"
FT BINDING 38
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 165
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 169
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
FT BINDING 230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02006"
SQ SEQUENCE 414 AA; 47699 MW; 945B29A5B79C5144 CRC64;
MSQNKLKTLI EELKKRKVFN NITSEEKVDL ITLDHGIYVG FDPTAISLHL GNYIQMVNLK
RFQNVGFKTI AILGGATSMI GDPSFKDSER KLLSNETILE NKKHIRKQLE NFGFKVIDNL
DFYKDMNILD YLRSVGKFFN VSTMMSRDSV ANRIQSGLSF TEFSYQTLQA YDFKVLCEKE
NVMMQLGGSD QWGNLVSGLD FINKTLSKNL PTIGITMNLL VDSNGNKIGK STGGASLWID
KTLTSPYVLY QYLLNTNDDD AYNLLLQLTF LQLSEIERIK NEHLKNPKLR LMQSRLSFEV
VKDIHGKEEA QRALHISTSL FKEKNSWFNL SLEDLIQLKG SVDFVPFKDD LFLTLVDSKI
ISSKREFNEF VRDKSLKING QDVTGLDYDL PWENYDNKYL ILKKGKKQYW VIYK
