ID   SYY_AYWBP               Reviewed;         413 AA.
AC   Q2NJG7;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Tyrosyl-tRNA synthetase;
DE            EC=6.1.1.1;
DE   AltName: Full=Tyrosine--tRNA ligase;
DE            Short=TyrRS;
GN   Name=tyrS; OrderedLocusNames=AYWB_309;
OS   Aster yellows witches'-broom phytoplasma (strain AYWB).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Candidatus Phytoplasma;
OC   Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=322098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16672622; DOI=10.1128/JB.188.10.3682-3696.2006;
RA   Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A.,
RA   Shevchenko D.V., Tsukerman K., Walunas T., Lapidus A., Campbell J.W.,
RA   Hogenhout S.A.;
RT   "Living with genome instability: the adaptation of phytoplasmas to
RT   diverse environments of their insect and plant hosts.";
RL   J. Bacteriol. 188:3682-3696(2006).
CC   -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a
CC       two-step reaction: tyrosine is first activated by ATP to form Tyr-
CC       AMP and then transferred to the acceptor end of tRNA(Tyr) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP +
CC       diphosphate + L-tyrosyl-tRNA(Tyr).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. TyrS type 1 subfamily.
CC   -!- SIMILARITY: Contains 1 S4 RNA-binding domain.
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DR   EMBL; CP000061; ABC65426.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_456505.1; -.
DR   GeneID; 3865903; -.
DR   GenomeReviews; CP000061_GR; AYWB_309.
DR   KEGG; ayw:AYWB_309; -.
DR   HOGENOM; Q2NJG7; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_02006; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002305; aa-tRNA-synth_Ib.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002942; S4_RNA_bd.
DR   InterPro; IPR002307; Tyr-tRNA-synth_Ib_bac/mito.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR11766; Tyr_tRNA-synt_1b; 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; FALSE_NEG.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis; RNA-binding.
FT   CHAIN         1    413       Tyrosyl-tRNA synthetase.
FT                                /FTId=PRO_0000234666.
FT   DOMAIN      347    413       S4 RNA-binding.
FT   MOTIF        39     48       "HIGH" region.
FT   MOTIF       225    229       "KMSKS" region.
FT   BINDING      34     34       Tyrosine (By similarity).
FT   BINDING     164    164       Tyrosine (By similarity).
FT   BINDING     168    168       Tyrosine (By similarity).
FT   BINDING     228    228       ATP (By similarity).
SQ   SEQUENCE   413 AA;  47600 MW;  C8C3BEA5A2B0A12F CRC64;
     MSFYEELKWR NLIKDCNNEI QVKELLDNNQ VKFYCGFDPT SHSLTVGHLI QITMILLMQR
     QGHLPVILVG GATGLIGDPK ETEERKLLSL ENSLQNAKSI ESQLKTILLN KQVEFVNNYQ
     WLSQIDIISF LRNYGKFFNI NYMLSKHVVA KRLASGISFT EFSYMILQSL DFHHLYKNHK
     VRLQLGGSDQ WGNITSGLEI IRKLEKKSDA LGVSTPLLLN SDGTKFGKSE KRVLWLNPLM
     TSPYEIYQYF LNVSDKEVIN YLKMLTLIPK KGILELEKKT LENPQKRLAQ KALTQSIINL
     IHSSDILQEC IKTNQILFSN AKKESFQEKD FILLQKTLFC HSIKEDILLV DALVQTKLAT
     SKSEAREFIK DNTIKLFNQK IKSLDFIITK ENTLFGKYIL LKKGKKNNAL IVF
//