ID SYE2_EHRCR Reviewed; 469 AA. AC Q2GGL8; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 01-MAY-2007, entry version 10. DE Glutamyl-tRNA synthetase 2 (EC 6.1.1.17) (Glutamate--tRNA ligase 2) DE (GluRS 2). GN Name=gltX2; Synonyms=gltX-2; OrderedLocusNames=ECH_0605; OS Ehrlichia chaffeensis (strain Arkansas). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=205920; 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:E21-E21(2006). 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000236; ABD45013.1; -; Genomic_DNA. DR GenomeReviews; CP000236_GR; ECH_0605. DR KEGG; ech:ECH_0605; -. DR TIGR; ECH_0605; -. 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; IPR004527; GltX_bac. DR InterPro; IPR000924; Glu_tRNA-synt_1c. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR001412; tRNA-synt_I. DR InterPro; IPR008925; tRNA_synt_bd. DR Gene3D; G3DSA:1.10.1160.10; G3DSA:1.10.1160.10; 1. 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 PANTHER; PTHR10119:SF1; PTHR10119:SF1; 1. DR Pfam; PF00749; tRNA-synt_1c; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR TIGRFAMs; TIGR00464; gltX_bact; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; KW Nucleotide-binding; Protein biosynthesis. FT CHAIN 1 469 Glutamyl-tRNA synthetase 2. FT /FTId=PRO_0000237363. FT MOTIF 11 21 "HIGH" region. FT MOTIF 238 242 "KMSKS" region. FT BINDING 241 241 ATP (By similarity). SQ SEQUENCE 469 AA; 54319 MW; FC59CCB762FB49A0 CRC64; MSHNVITRFA PSPTGHLHLG GARTALFNWL YAKHNNGKFL LRIEDTDKKR SSKELIDSII NAMSWLKIPY DGEIVLQSKN ISRHIEIANQ LILNNKAYYC YCSEEEINKE KEEFSKKGLY YKHNCIWKNK NFTIDNLTRV IRLRSPTEGV TSFDDKVYGN ITVSNTQLDD MVLLRSDNTP TYLLSVVVDD HDMNITHIIR GTDHLTNTAR QLLIYNALEW NPPKFAHIPL IHDEDGNKLS KRHQAIGIHE YKNLGILPEA ISNYLLRMGW SHEDDEIISM DQAIKWFSIK NIGQSPARLD NKKLEFLNNH YISLTEDEVI LNMIIPIIEK KIGYMLNEVK KGYLLKGLYE LKKRTKNLVN LANESLFYVE DVPISIDQEA SAIIKDYKHV FSILYNNLSR ISEKEWNNSI LTSTIKNISQ NLDIKISNIY HCLRASIVGR MNAPSIIEIM INLQQEECLK RIKYAQNIE //