ID A0A9X3IAE9_9SPHI Unreviewed; 547 AA. AC A0A9X3IAE9; DT 08-NOV-2023, integrated into UniProtKB/TrEMBL. DT 08-NOV-2023, sequence version 1. DT 27-MAR-2024, entry version 3. 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 ORFNames=OQZ29_18730 {ECO:0000313|EMBL:MCX3266801.1}; OS Pedobacter agri. OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales; OC Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=454586 {ECO:0000313|EMBL:MCX3266801.1, ECO:0000313|Proteomes:UP001142592}; RN [1] {ECO:0000313|EMBL:MCX3266801.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 19486 {ECO:0000313|EMBL:MCX3266801.1}; RA Graham C., Newman J.D.; RL Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases. 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00253}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MCX3266801.1}. 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; JAPJUH010000005; MCX3266801.1; -; Genomic_DNA. DR RefSeq; WP_010600609.1; NZ_JAPJUH010000005.1. DR Proteomes; UP001142592; Unassembled WGS sequence. 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}. FT DOMAIN 152..447 FT /note="Aminoacyl-transfer RNA synthetases class-II family FT profile" FT /evidence="ECO:0000259|PROSITE:PS50862" FT BINDING 103 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253" FT BINDING 245 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253" FT BINDING 277..279 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253" FT BINDING 292..296 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253" FT BINDING 359..360 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253" FT BINDING 405..409 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253" FT BINDING 409..412 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00253" SQ SEQUENCE 547 AA; 63401 MW; 928E8921425211FA CRC64; MAQKNNDEQF KNVISHAKEY GFVFQSSEIY DGLSAVYDYG QLGAELKNNI KTYWWKAMVQ MHENIVGIDS AIFMHPKVWK ASGHVDGFND PMIDNKDSKK RYRADQLLEN KIDELYSELA NFSADNKAKF EEFQQEILGL SDEGQAAWVP SFKDEEGILD NAKYPFVDEA SWRFVKKGLT LEVEMNLALK SGNLTQLKDL IVDYKVICPI SKTSNWTDVR QFNLMFSTQF GAMAEGSDEV YLRPETAQGI FVNFLNVQKS GRMKIPFGIA QIGKAFRNEV IARQFIMRMR EFEQMEMQFF VRPGEDKKWF EYWKEARLKW HKALGTAPEK YRYHDHVKLA HYANAATDIE FEFPFGFKEV EGIHSRTDFD LTQHQQYSGK KMQYFDNDLN EEGKPYGNYV PYVIETSIGL DRMFLLTMIN AFEEQDLSTE DKQDSRTLLR LHPALAPYKV AVFPLTKKDG LPEKAREIMD ALKFDFNCIY EEKDAIGKRY RRQDAIGTPF CITVDHQSLE DNTVTIRHRD SMEQERIAIA DLGTIVGNAV SWKNLLA //