ID   SYEM_MACFA              Reviewed;         506 AA.
AC   Q4R4F1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Probable glutamyl-tRNA synthetase, mitochondrial;
DE            EC=6.1.1.17;
DE   AltName: Full=Glutamate--tRNA ligase;
DE            Short=GluRS;
DE   Flags: Precursor;
GN   Name=EARS2; ORFNames=QtsA-10185;
OS   Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; AB178963; BAE02014.1; -; mRNA.
DR   HOVERGEN; Q4R4F1; -.
DR   BRENDA; 6.1.1.17; 3438.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
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   PANTHER; PTHR10119; Glu_tRNA-synt_1c; 1.
DR   TIGRFAMs; TIGR00464; gltX_bact; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; RNA-binding;
KW   Transit peptide.
FT   TRANSIT       1     41       Mitochondrion (Potential).
FT   CHAIN        42    506       Probable glutamyl-tRNA synthetase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000254561.
FT   NP_BIND     284    288       ATP (By similarity).
FT   REGION       40     42       Glutamate binding (By similarity).
FT   REGION      228    232       Glutamate binding (By similarity).
FT   MOTIF        45     53       "HIGH" region.
FT   MOTIF       284    288       "KMSKS" region.
FT   BINDING      50     50       ATP (By similarity).
FT   BINDING      76     76       Glutamate (By similarity).
FT   BINDING     246    246       Glutamate (By similarity).
FT   BINDING     249    249       ATP (By similarity).
SQ   SEQUENCE   506 AA;  56865 MW;  314400085FF645F6 CRC64;
     MAALLRRLLQ RGRPLAASGR RVGRREARLG TGPGVAVRVR FAPSPTGFLH LGGLRTALYN
     YIFAKKYQGS FILRLEDTDQ TRFVPGAAEN IENMLEWAGI PPDESPRRGG PAGPYQQSQR
     LELYAQATEA LLKTGAAYPC FCSPQRLELL KKEALRNHQM PRYDNRCRNM SQEQVAQKLA
     KDPKPAIRFR LEQAAPAFED LVYGWNRHDV ASVEGDPVIM KSDGFPTYHL ACVVDDHHMG
     ISHVLRGSEW LISTAKHLLL YQALGWHPPH FAHLPLLLNR DGSKLSKRQG DIFLEHFAAE
     GFLPDSLLDI ITNCGSGFAE NQMGRTLPEL ITQFNLTRVT CHSALLDLEK LPEFNRLHLQ
     RLVNNESQRC QLVEKLQALV EEAFGSQLQN RDVLNPIYME RILLLRQGHI CRLQDLVSPV
     YSYLWTRPSV GRAQLDAISE EVDVIAKRVL GLLERSGMSL TQDMLSGELK KLSEGLEGTK
     HSNVMKLLRV ALSGQQALSS MFKVQG
//