ID A0A0M4GU38_9GAMM Unreviewed; 689 AA.
AC A0A0M4GU38;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00255};
DE AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00255};
GN Name=glyS {ECO:0000256|HAMAP-Rule:MF_00255};
GN ORFNames=AMQ28_06290 {ECO:0000313|EMBL:ALD02010.1};
OS Acinetobacter sp. TTH0-4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1646498 {ECO:0000313|EMBL:ALD02010.1, ECO:0000313|Proteomes:UP000055186};
RN [1] {ECO:0000313|EMBL:ALD02010.1, ECO:0000313|Proteomes:UP000055186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTH0-4 {ECO:0000313|EMBL:ALD02010.1,
RC ECO:0000313|Proteomes:UP000055186};
RA Zhang G.;
RT "Acinetobacter qinghaiensis sp. nov., isolated from active layer of
RT permafrost region.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000201,
CC ECO:0000256|HAMAP-Rule:MF_00255};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00255}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00255}.
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DR EMBL; CP012608; ALD02010.1; -; Genomic_DNA.
DR RefSeq; WP_053578875.1; NZ_CP012608.1.
DR AlphaFoldDB; A0A0M4GU38; -.
DR STRING; 1646498.AMQ28_06290; -.
DR KEGG; att:AMQ28_06290; -.
DR PATRIC; fig|1646498.3.peg.1278; -.
DR Proteomes; UP000055186; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
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:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR NCBIfam; TIGR00211; glyS; 1.
DR PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01045; TRNASYNTHGB.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00255};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00255}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00255};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00255};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00255}.
FT DOMAIN 581..680
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 689 AA; 75432 MW; AB61DEC6B6D3BBDF CRC64;
MSKHTVLFEL GCEELPPKSL KKLRDALHTE TVKGLKDAGL AFDSIEAYAA PRRLALKIVN
VDAAQADTQK RFDGPAKQAA FDAEGHPTKA LEGFMRGQGI TVEQVTTFQA GKVEKVCYLK
DVKGQSLDIL LPQILQNALD NLPIAKRMRS AASRTEFVRP VKWVVLLKDN DVIEATIQDI
QTGNLTFGHR FHAPEAITLG HADEYLMKLK TAYVVANFEE RQAIIDGQVK ALADEVNAIA
IVPSDLRDEV TALVEWPVAL RASFEERFLA VPQEALITTM QDNQKYFCLV NSDNKLQPYF
ITVSNIESKD PAQIIEGNEK VVRPRLSDAE FFFLQDQKQP LASRKEKLAN MVFQAQLGTL
WDKSTRIAKL AVALAPITGA NATDAEKAAL LAKCDLTSEL VGEFPELQGI AGTYYARLEG
ENAEVSDALG EQYLPKFAGD VLPKTKTGTT IALADRLDTL TGIFGIGQAP TGSKDPFALR
RSAIGILRLV TENELDVSIE DLIQLALNAY GDVVADHAKT LTDAVNFLEG RYRAKYEDQG
VAVDVIQAVQ ALSPKSPLDF DKRVTAVNHF RDLPEAAALA AANKRVANIL AKEAEPTGAV
VEANLVEEAE KALFAVLAKI TPEVEPLFAS KEYTEALSKL AALRAPVDAF FDSVMVMADD
AELKANRLRL LVQLRDLFTK VADISVLQH
//
