ID SYG_MYCPA Reviewed; 463 AA. AC Q73Y21; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAY-2015, entry version 77. DE RecName: Full=Glycine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00253}; DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00253}; DE AltName: Full=Glycyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00253}; DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00253}; GN Name=glyQS {ECO:0000255|HAMAP-Rule:MF_00253}; Synonyms=glyS; GN OrderedLocusNames=MAP_2137c; OS Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium avium complex (MAC). OX NCBI_TaxID=262316; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-968 / K-10; RX PubMed=16116077; DOI=10.1073/pnas.0505662102; RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., RA Banerji N., Kanjilal S., Kapur V.; RT "The complete genome sequence of Mycobacterium avium subspecies RT paratuberculosis."; RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005). CC -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly). CC {ECO:0000255|HAMAP-Rule:MF_00253}. CC -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate CC + glycyl-tRNA(Gly). {ECO:0000255|HAMAP-Rule:MF_00253}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00253}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00253}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00253}. 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; AE016958; AAS04454.1; -; Genomic_DNA. DR RefSeq; NP_961071.1; NC_002944.2. DR RefSeq; WP_010949492.1; NC_002944.2. DR ProteinModelPortal; Q73Y21; -. DR STRING; 262316.MAP2137c; -. DR EnsemblBacteria; AAS04454; AAS04454; MAP_2137c. DR GeneID; 2720577; -. DR KEGG; mpa:MAP2137c; -. DR PATRIC; 17996894; VBIMycAvi108102_2271. DR eggNOG; COG0423; -. DR KO; K01880; -. DR OMA; HKRFRAD; -. DR OrthoDB; EOG6R87F8; -. DR BioCyc; MAVI262316:GCQR-2163-MONOMER; -. DR Proteomes; UP000000580; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004820; F:glycine-tRNA ligase activity; ISS:UniProtKB. DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB. DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.800; -; 1. DR HAMAP; MF_00253_B; Gly_tRNA_synth_B; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR027031; Gly-tRNA_synthase/POLG2. DR InterPro; IPR022961; Gly_tRNA_ligase_bac. DR InterPro; IPR002315; tRNA-synt_gly. DR PANTHER; PTHR10745; PTHR10745; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PRINTS; PR01043; TRNASYNTHGLY. DR SUPFAM; SSF52954; SSF52954; 1. DR TIGRFAMs; TIGR00389; glyS_dimeric; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 463 Glycine--tRNA ligase. FT /FTId=PRO_0000072966. FT NP_BIND 197 199 ATP. {ECO:0000255|HAMAP-Rule:MF_00253}. FT NP_BIND 207 212 ATP. {ECO:0000255|HAMAP-Rule:MF_00253}. FT NP_BIND 284 285 ATP. {ECO:0000255|HAMAP-Rule:MF_00253}. FT NP_BIND 328 331 ATP. {ECO:0000255|HAMAP-Rule:MF_00253}. FT REGION 212 216 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00253}. FT REGION 324 328 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00253}. FT BINDING 102 102 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00253}. FT BINDING 165 165 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00253}. SQ SEQUENCE 463 AA; 52971 MW; F602B4C500CFEB2D CRC64; MHRLVASVID TVVNLAKRRG FVYPSGEIYG GTRSAWDYGP LGVEFKENIK RQWWRSVVTG REDVVGLDSS IILPRQVWVA SGHVEVFHDP LVESLITHKR YRADHLIEAY EAKHGHPPPN GLADIRDPDT GEPGRWTEPR EFNMMLKTYL GPIETEEGLH YLRPETAQGI FVNFANVVTT ARKKPPFGIG QIGKSFRNEI TPGNFIFRTR EFEQMEMEFF VEPSTAKEWH QYWIDTRLQW YVELGIDPQN LRLFEHPADK LSHYSDRTVD IEYKFGFAGN PWGELEGVAN RTDFDLSTHS KHSGVDLSFY DQATDSRYIP YVIEPAAGLT RSFMAFLIDA YVEDEAPNAK GKMEKRAVLR LDPRLAPVKA AVLPLSRHAD LSPKARDLAA ELRRFWNIEF DDAGAIGRRY RRQDEIGTPF CVTVDFDSLE DNAVTVRRRD DMSQERIGMD AVADYLSARL KGC //