ID   SYY_ANAPZ               Reviewed;         412 AA.
AC   Q2GIN1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 29.
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=APH_1244;
OS   Anaplasma phagocytophilum (strain HZ).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=212042;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S.,
RA   Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N.,
RA   Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P.,
RA   Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F.,
RA   Forberger H., Halpin R., Mulligan S., Robinson J., White O.,
RA   Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(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.
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; CP000235; ABD43829.1; -; Genomic_DNA.
DR   RefSeq; YP_505770.1; -.
DR   GeneID; 3930514; -.
DR   GenomeReviews; CP000235_GR; APH_1244.
DR   KEGG; aph:APH_1244; -.
DR   NMPDR; fig|212042.5.peg.1192; -.
DR   TIGR; APH_1244; -.
DR   HOGENOM; Q2GIN1; -.
DR   OMA; Q2GIN1; TDPTGDS.
DR   BioCyc; APHA212042:APH_1244-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; 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; 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    412       Tyrosyl-tRNA synthetase.
FT                                /FTId=PRO_1000088575.
FT   DOMAIN      343    409       S4 RNA-binding.
FT   MOTIF        43     52       "HIGH" region.
FT   MOTIF       230    234       "KMSKS" region.
FT   BINDING      38     38       Tyrosine (By similarity).
FT   BINDING     170    170       Tyrosine (By similarity).
FT   BINDING     174    174       Tyrosine (By similarity).
FT   BINDING     233    233       ATP (By similarity).
SQ   SEQUENCE   412 AA;  45726 MW;  82C86389EE3D73FA CRC64;
     MEFNSEFLAT LCARGYLHQL TDATALDGIM SSGAVTAYIG FDCTANSLHI GSLMQIMLLR
     YLQRFGHKPI VLLGGATTKV GDPSGKEKTR AMLSEDNISA NKEGILRVIK KFLSEDVVVV
     DNAEWLGNYG YLDFLREIGS KFSVNVMLGL ESVKSRLSRD QQLSFLEFSY VLLQSYDFVE
     LHKRYGCILQ IGGSDQWGNI VSGIDLARKM GCPQLYGVTT PLLLNSSGAK MGKTADGAIW
     LDETLYSPYN YWQYFRNVPD QDVGRLLRLF TELPLSEIER LEALKGEELN EAKKILATAV
     TSICHGAEVA LQVENQALKV FEHNDHDELR SITFSRKTLG QGIPISKLLH MWGLEESISA
     GRRLIRGGGC KINGGVVLDE EKLLNCGDFD DNGGYVAVFC GKKRRLKVVL ED
//