ID C6WRG6_ACTMD Unreviewed; 461 AA. AC C6WRG6; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAR-2024, entry version 89. DE RecName: Full=Glycine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00253}; DE EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00253}; DE AltName: Full=Glycyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00253}; DE Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00253}; GN Name=glyQS {ECO:0000256|HAMAP-Rule:MF_00253}; GN OrderedLocusNames=Amir_1266 {ECO:0000313|EMBL:ACU35218.1}; OS Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 OS / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101). OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales; OC Pseudonocardiaceae; Actinosynnema. OX NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU35218.1, ECO:0000313|Proteomes:UP000002213}; RN [1] {ECO:0000313|EMBL:ACU35218.1, ECO:0000313|Proteomes:UP000002213} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 / RC NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213}; RX PubMed=21304636; DOI=10.4056/sigs.21137; RA Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G., RA Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L., RA Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K., RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T., RA Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Actinosynnema mirum type strain (101)."; RL Stand. Genomic Sci. 1:46-53(2009). CC -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly). CC {ECO:0000256|HAMAP-Rule:MF_00253}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl- CC tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA- CC COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215; CC EC=6.1.1.14; Evidence={ECO:0000256|HAMAP-Rule:MF_00253}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00253}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00253}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|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; CP001630; ACU35218.1; -; Genomic_DNA. DR RefSeq; WP_015800108.1; NC_013093.1. DR AlphaFoldDB; C6WRG6; -. DR STRING; 446462.Amir_1266; -. DR KEGG; ami:Amir_1266; -. DR eggNOG; COG0423; Bacteria. DR HOGENOM; CLU_015515_2_1_11; -. DR OrthoDB; 9760853at2; -. DR Proteomes; UP000002213; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00774; GlyRS-like_core; 1. DR CDD; cd00858; GlyRS_anticodon; 1. DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1. DR HAMAP; MF_00253_B; Gly_tRNA_synth_B; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR036621; Anticodon-bd_dom_sf. DR InterPro; IPR027031; Gly-tRNA_synthase/POLG2. DR InterPro; IPR022961; Gly_tRNA_ligase_bac. DR InterPro; IPR033731; GlyRS-like_core. DR InterPro; IPR002315; tRNA-synt_gly. DR NCBIfam; TIGR00389; glyS_dimeric; 1. DR PANTHER; PTHR10745:SF0; GLYCINE--TRNA LIGASE; 1. DR PANTHER; PTHR10745; GLYCYL-TRNA SYNTHETASE/DNA POLYMERASE SUBUNIT GAMMA-2; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PRINTS; PR01043; TRNASYNTHGLY. DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00253}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00253}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00253}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00253}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00253}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00253}; Reference proteome {ECO:0000313|Proteomes:UP000002213}. FT DOMAIN 4..365 FT /note="Aminoacyl-transfer RNA synthetases class-II family FT profile" FT /evidence="ECO:0000259|PROSITE:PS50862" FT BINDING 99 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253" FT BINDING 163 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253" FT BINDING 195..197 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253" FT BINDING 205..210 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253" FT BINDING 210..214 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253" FT BINDING 282..283 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253" FT BINDING 322..326 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253" FT BINDING 326..329 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253" SQ SEQUENCE 461 AA; 52682 MW; 7049E38ECC4E0AD0 CRC64; MAVDRIETVV SLCKRRGFVY PCGEIYGGTR SAWDYGPLGV ELKDNIKRQW WNFMVRGRED VVGLDSSVIL PREVWTASGH VEAFVDPLVE CNSCHKRFRQ DTLSEEYAER TGKDVAEGDV SDVPCPNCGT RGQYTEPRMF NGLLKTHLGP VETEEGLHYL RPETAQGIFT NFLNVQTTSR RKPPFGIGQI GKSFRNEITP GNFIFRTREF EQMEMEFFVE PGTDEQWHQY WIDERTRWYT ELGISADNLR HYEHPAEKLS HYAKRTVDIE YRFRFGGQEW GELEGIANRT DFDLTTHSNH SGVDLSYFDQ ATNSRYRPFV IEPAAGVGRP MMAFLLEAYT EDEAPNAKGG VDKRVVLRLD RRLAPVKAAV LPLSRNADLS PKAKDLAAAL RKHWNVEFDD AGAIGRRYRR QDEIGTPFCV TVDFDTLTDH AVTVRERDTM SQERVSMDQI EGYLAARLIG A //