ID A0A1X6YAG9_9RHOB Unreviewed; 686 AA.
AC A0A1X6YAG9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ECO:0000313|EMBL:SLN15363.1};
GN ORFNames=CLV79_103201 {ECO:0000313|EMBL:PSK87152.1}, LOS8367_00198
GN {ECO:0000313|EMBL:SLN15363.1};
OS Limimaricola soesokkakensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Limimaricola.
OX NCBI_TaxID=1343159 {ECO:0000313|EMBL:SLN15363.1, ECO:0000313|Proteomes:UP000193495};
RN [1] {ECO:0000313|EMBL:SLN15363.1, ECO:0000313|Proteomes:UP000193495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8367 {ECO:0000313|EMBL:SLN15363.1,
RC ECO:0000313|Proteomes:UP000193495};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSK87152.1, ECO:0000313|Proteomes:UP000240624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29956 {ECO:0000313|EMBL:PSK87152.1,
RC ECO:0000313|Proteomes:UP000240624};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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; PYGB01000003; PSK87152.1; -; Genomic_DNA.
DR EMBL; FWFY01000001; SLN15363.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6YAG9; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000193495; Unassembled WGS sequence.
DR Proteomes; UP000240624; Unassembled WGS sequence.
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 575..674
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 686 AA; 74770 MW; 67EC54DD031D1454 CRC64;
MPDLLIELFS EEIPARMQAR AAEDLKRMVT DGLVEAGLTY ASAGAFHTPR RLALSVEGLS
EASRDTVEER KGPRTDAPEK ALEGFLRSTG LTMDQLEIRD EKKGQAYFAK ITHKGRPAEE
IVAEVLEGAI RNFPWPKSMR WGAGDLRWVR PLHSILCLLS DEQGARVVPM EIDGIAAGDV
TRGHRFMGPD EFTVSSFEDY EAKLKRGCVL LRAEERAETI WSEASSQAFA QGLELVEDRG
LLDEVAGLVE WPVVLMGEIG DEFLDLPPEV LQTSMKEHQK FFSVRDPKSG KITRFVTVAN
IETRDHGATI LAGNGKVLAA RLSDAKFFWE NDLRVVKEGG LEAMGEGLSN VTFHNRLGSQ
SDRVARIAAL AREIAPRVSA DADDAERAAK VAKADLRSEM VGEFPELQGL MGRYYAEAQG
LSPAIAAAAQ EHYQPLGPSD DVPSAPVSVA VALADKLDTL AGFWAIEEKP TGSKDPFALR
RAALGVIRLV LSNGLRLQLR ELIAKADGHA EVEDLLSFFH DRLKVHLRAE GIPHDVIDAC
IAMPGNDDLT LLVARAEALA GFLKTEDGEN LTQGFKRANN ILTQAEQKDG VEYSFGADAK
FAEGSEEKAL FAALDGAQPK IDAAMASEDF ASAMAAMASL RAPIDAFFEA VQVNTENQVL
RRNRLNLLSR IRTTCGSVAD LSKIEG
//
