ID   SYY_ANAVT               Reviewed;         398 AA.
AC   Q3MEN7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=Ava_0925;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 2 subfamily.
CC   -!- SIMILARITY: Contains 1 S4 RNA-binding domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000117; ABA20549.1; -; Genomic_DNA.
DR   RefSeq; YP_321444.1; -.
DR   GeneID; 3681299; -.
DR   GenomeReviews; CP000117_GR; Ava_0925.
DR   KEGG; ava:Ava_0925; -.
DR   NMPDR; fig|240292.3.peg.131; -.
DR   HOGENOM; Q3MEN7; -.
DR   OMA; Q3MEN7; YVVQVGK.
DR   BioCyc; AVAR240292:AVA_0925-MON; -.
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_02007; -; 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; 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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis; RNA-binding.
FT   CHAIN         1    398       Tyrosyl-tRNA synthetase.
FT                                /FTId=PRO_0000236690.
FT   DOMAIN      334    398       S4 RNA-binding.
FT   MOTIF        48     57       "HIGH" region.
FT   MOTIF       235    239       "KMSKS" region.
FT   BINDING     238    238       ATP (By similarity).
SQ   SEQUENCE   398 AA;  44447 MW;  85E4BC864466B926 CRC64;
     MAENFSWLHR GIAEVFPQPT DAESDIESLE KRLATTDRPL RVKYGIDPTG ADIHLGHSIP
     MRKLRGFQDA GHTAVLIIGD FTARIGDPTG KSEMRRQLTE EDVKQNAQTY LDQVRPILDF
     DTPGRLEVRY NSEWLSRLDL GKITELLATM TVGQMLAKEG FADRYKKENP IFLHEFLYPL
     MQGYDSVAIE ADVELGGTDQ KFNIAVGRDL QRHFGQKPQF GVLLPILIGT DGVQKMSKSL
     GNYVSLSEHP GQKYQKLQGV PDQMLEQYFE LLTDLPIDKL PANPRDRQML LAWEIVKQYH
     GEQAAQEAKE AAQSGGKEGA VPEFSLAGVP QFPVKLAYLL GATGLCKSTG EGKRKIQEGG
     VRLDGDRISD ADTIFQQPDE LQGRVLQVGK NKFVRLVL
//