ID SYGA_ANADE Reviewed; 309 AA. AC Q2IQJ6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 22. DE RecName: Full=Glycyl-tRNA synthetase alpha subunit; DE EC=6.1.1.14; DE AltName: Full=Glycine--tRNA ligase alpha subunit; DE Short=GlyRS; GN Name=glyQ; OrderedLocusNames=Adeh_1305; OS Anaeromyxobacter dehalogenans (strain 2CP-C). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=290397; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., RA Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., RA Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate CC + glycyl-tRNA(Gly). CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the class-II 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; CP000251; ABC81079.1; -; Genomic_DNA. DR RefSeq; YP_464516.1; -. DR GeneID; 3888660; -. DR GenomeReviews; CP000251_GR; Adeh_1305. DR KEGG; ade:Adeh_1305; -. DR HOGENOM; Q2IQJ6; -. DR OMA; Q2IQJ6; CRRPTDG. DR BioCyc; ADEH290397:ADEH_1305-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:HAMAP. DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:HAMAP. DR HAMAP; MF_00254; -; 1. DR InterPro; IPR006194; Gly-tRNA-synth_II_heterodimer. DR InterPro; IPR002310; Gly-tRNA_synth_IIc_asu. DR Pfam; PF02091; tRNA-synt_2e; 1. DR PRINTS; PR01044; TRNASYNTHGA. DR ProDom; PD006985; tRNA_synt_2e; 1. DR TIGRFAMs; TIGR00388; glyQ; 1. DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis. FT CHAIN 1 309 Glycyl-tRNA synthetase alpha subunit. FT /FTId=PRO_1000047395. SQ SEQUENCE 309 AA; 35324 MW; C997716B21ED4CF5 CRC64; MYFQDLILKL QSYWASRNCI LAQGYDQEVG AGTMNPSTFL RVLGPEPWNV AYVEPSRRPA DGRYGENPNR LYQHHQFQVI LKPNPPDVQE LYLGSLRAIG IDPREHDIRF VEDDWESPTL GAWGLGWEVW CDGMEITQYT YFQQAGGFEV KPVAAELTYG LERIAMYLQD VENVFDVEWV KGVKYREVFH RNEVEMSTYS FQASDPKMLF GLFDTYEAEC KRLIGLKLPL PAYDYCLKCS HAFNNLDARG AISVTERAAY IGRVRALAHD CAKGYLDSRE ALGFPLLPPA DRKQAVEAAR AAREARESR //