ID   SYY_ANADE               Reviewed;         420 AA.
AC   Q2IPT7;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
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=Adeh_1044;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
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., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) 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 1 subfamily.
CC   -!- SIMILARITY: Contains 1 S4 RNA-binding domain.
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DR   EMBL; CP000251; ABC80819.1; -; Genomic_DNA.
DR   RefSeq; YP_464256.1; -.
DR   GeneID; 3888470; -.
DR   GenomeReviews; CP000251_GR; Adeh_1044.
DR   KEGG; ade:Adeh_1044; -.
DR   HOGENOM; Q2IPT7; -.
DR   OMA; Q2IPT7; PGYVPNT.
DR   BioCyc; ADEH290397:ADEH_1044-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_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   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    420       Tyrosyl-tRNA synthetase.
FT                                /FTId=PRO_0000234664.
FT   DOMAIN      353    419       S4 RNA-binding.
FT   MOTIF        38     47       "HIGH" region.
FT   MOTIF       227    231       "KMSKS" region.
FT   BINDING      33     33       Tyrosine (By similarity).
FT   BINDING     167    167       Tyrosine (By similarity).
FT   BINDING     171    171       Tyrosine (By similarity).
FT   BINDING     230    230       ATP (By similarity).
SQ   SEQUENCE   420 AA;  45350 MW;  BB93A25BBA1431C1 CRC64;
     MQNLLEALVP RSLVHDQTPG LQARLAQGPI TGYVGFDPTA DSLHVGHLLA VMSLAWLQRC
     GGTPIIVVGG GTGMVGDPSG KRSERPVLSV EEIDRNVAAI RAQLERFVSF EGQNAARVRN
     NADWLRSIGL MEFLRDVGKH FTVNYMLAKD SVKGRMESGI SFTEFSYQLI QAYDFWHLFH
     AERCELQMGG SDQWGNITAG AELVSRKDGA SVHGLTFPLL TTASGTKFGK TEGGAVWLDP
     ARTSPYKFFQ FWLNTDDRDV ERLLKFFTFL SLDEIAALLA EQARDPGKRP AQRRLAEDVT
     ARVHGPDVTR SVIEASRILF GGTDLRAAGV DVLDVLAGEI PSATVTGDEL AALTVADLLV
     KVGLAASKGE VRRGVAGRGF SLNGAVLESG DAKVAAGELL AGGYALLQKG KRNYALVKVR
//