ID SYEM_DANRE Reviewed; 503 AA. AC Q0P499; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 25. 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=zgc:153247; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (AUG-2006) 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. 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; BC122204; AAI22205.1; -; mRNA. DR IPI; IPI00786651; -. DR RefSeq; NP_001038907.1; -. DR UniGene; Dr.83804; -. DR PRIDE; Q0P499; -. DR GeneID; 751732; -. DR KEGG; dre:751732; -. DR ZFIN; ZDB-GENE-060825-214; zgc:153247. DR HOVERGEN; Q0P499; -. DR BRENDA; 6.1.1.17; 96826. DR Bgee; Q0P499; -. 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 22 Mitochondrion (Potential). FT CHAIN 23 503 Probable glutamyl-tRNA synthetase, FT mitochondrial. FT /FTId=PRO_0000254564. FT NP_BIND 265 269 ATP (By similarity). FT REGION 21 23 Glutamate binding (By similarity). FT REGION 209 213 Glutamate binding (By similarity). FT MOTIF 26 34 "HIGH" region. FT MOTIF 265 269 "KMSKS" region. FT BINDING 31 31 ATP (By similarity). FT BINDING 57 57 Glutamate (By similarity). FT BINDING 227 227 Glutamate (By similarity). FT BINDING 230 230 ATP (By similarity). SQ SEQUENCE 503 AA; 57023 MW; B5E856B44B303AD7 CRC64; MKILRGVSRQ MCTSRPEVRV RFAPSPTGFL HLGGLRTALY NFLFSRQRRG VFILRLEDTD QKRLVPGAAE HIEDMLEWAG IPPDESSRRG GDYGPYVQSE RLHLYTEAAS SLLNTGHAYY CFCSNQRLEL LKKEAQRSGH APRYDNRCRR LQPQQVEQKL AAGVPAVVRF KLHTGTEEFQ DLVFGWTGHA VGAVEGDPVI LKADGYPTYH LASVVDDHHM RISHVLRGCE WLISSAKHLQ LYRALRWTPP TYAHLPLLLN RDGSKLSKRQ GDIFLQSFRD RGVLPETLLD LVTHAGSGFS DNRMGRRLDE LIRDFNISKI TTHSALLDLD KLEEFSRLHL QRRIEDPQQC VWLCEELKQM VKHTHSSEIS AAAVLEPEYI ERVLQLRKGH ISSLQDLLSS THSYLWVRPR VSQTQLQSES AHAKDIATAV MQMVLAGGSL VSMERLSSEL KQISSRTNST HSSVMKVLRL LLSAQQRGPS VAEMMLSLGE QEVCVRLQKA LEL //