ID   SYE2_ANAPZ              Reviewed;         468 AA.
AC   Q2GKT8;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Glutamyl-tRNA synthetase 2;
DE            EC=6.1.1.17;
DE   AltName: Full=Glutamate--tRNA ligase 2;
DE            Short=GluRS 2;
GN   Name=gltX2; Synonyms=gltX-2; OrderedLocusNames=APH_0408;
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 glutamate to tRNA(Glu) in a
CC       two-step reaction: glutamate is first activated by ATP to form
CC       Glu-AMP and then transferred to the acceptor end of tRNA(Glu) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP +
CC       diphosphate + L-glutamyl-tRNA(Glu).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000235; ABD43300.1; -; Genomic_DNA.
DR   RefSeq; YP_505013.1; -.
DR   GeneID; 3930482; -.
DR   GenomeReviews; CP000235_GR; APH_0408.
DR   KEGG; aph:APH_0408; -.
DR   NMPDR; fig|212042.5.peg.396; -.
DR   TIGR; APH_0408; -.
DR   HOGENOM; Q2GKT8; -.
DR   OMA; Q2GKT8; NQCIDES.
DR   BioCyc; APHA212042:APH_0408-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00022; -; 1.
DR   InterPro; IPR008925; aa-tRNA-synth_I_codon-bd.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR004527; Glu-tRNA-synth_Ic_bac/mito.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Gene3D; G3DSA:1.10.10.350; tRNA_synt_bd; 1.
DR   PANTHER; PTHR10119; Glu_tRNA-synt_1c; 1.
DR   TIGRFAMs; TIGR00464; gltX_bact; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    468       Glutamyl-tRNA synthetase 2.
FT                                /FTId=PRO_0000237338.
FT   MOTIF         9     19       "HIGH" region.
FT   MOTIF       238    242       "KMSKS" region.
FT   BINDING     241    241       ATP (By similarity).
SQ   SEQUENCE   468 AA;  53152 MW;  CE21B305641F3D70 CRC64;
     MRVVTRFAPS PTGSLHLGGA RTALFNWLFA RHHKGKFLLR MEDTDKKRSS DVVVQSIIDD
     MSWLGLQHDG DIVVQSSRAA RHVAVARELV ELGRAYRCYC SEDEVNEQKL QSEGTGKYFR
     HVCPWKHLNS TGDLPNKPYV VRLKSPENTT IEFLDGVYGK ISVKSDQIDD MVILRSDGTP
     TYLLAVVVDD HDMEITHIIR GSDHITNTVK QIVLAEAMSW VSPKFFHIPL IHDENGAKLS
     KRNRAPGIHE YKEQGFLPEA LCNYLLRMGW SYQNKEIVSM QEAIALFSME DVGVSCSCLD
     YKKLVFLNHH YMGSKSESEI LDLLLPILEE KLGGRISEEK LSRLSLGIKQ LVERAKTLTD
     LAEDSLFYVQ DVEININPEA VETIQNSKKF LAELLESMSG IHPDMWKKTH LSSQIKEFSK
     TRNLAMSDVY HFLRASITGR LQSPNISEVM EILGQEMCIN RMLSAQEI
//