ID A0A1Q8YFW1_9BURK Unreviewed; 733 AA.
AC A0A1Q8YFW1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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:OLP06799.1};
GN ORFNames=BLL52_1910 {ECO:0000313|EMBL:OLP06799.1};
OS Rhodoferax antarcticus ANT.BR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=1111071 {ECO:0000313|EMBL:OLP06799.1, ECO:0000313|Proteomes:UP000185911};
RN [1] {ECO:0000313|EMBL:OLP06799.1, ECO:0000313|Proteomes:UP000185911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANT.BR {ECO:0000313|EMBL:OLP06799.1,
RC ECO:0000313|Proteomes:UP000185911};
RA Baker J., Riester C., Skinner B., Newell A., Swingley W., Madigan M.,
RA Jung D., Asao M., Chen M., Loughlin P., Pan H., Lin S., Li N., Shaw J.,
RA Prado M., Sherman C., Li X., Tang J., Blankenship R., Zhao T., Touchman J.,
RA Sattley M.;
RT "Genome sequence of Rhodoferax antarcticus ANT.BR, a psychrophilic purple
RT nonsulfur bacterium from an Antarctic microbial mat.";
RL Submitted (JAN-2017) 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}.
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:OLP06799.1}.
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DR EMBL; MSYM01000012; OLP06799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8YFW1; -.
DR STRING; 81479.RA876_03955; -.
DR Proteomes; UP000185911; 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}; Reference proteome {ECO:0000313|Proteomes:UP000185911}.
FT DOMAIN 622..723
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 733 AA; 78109 MW; 56B45688D2F801AD CRC64;
MFVEELPPKA LKKLGEAFAG QLADQLRALG LASAESVVTP FASPRRLAAH ITHVAAKAAD
KAVQQKLMPV NVGLSADGLA TPALLKKLQA LGADVSDPVF AVAALRKAAD GKAEALFYDS
LVDGATLEVG LQQALDVALA KLPIPKVMSY QLEADCELPG WSSVNFVRPA HGLVALHSDT
VVPVKVLGLT AGNTTLGHRF EAAKSPVVLA NADSYAQALR DDGAVIASFA ERRAAIVQQL
KQAAALVGPA VSAIEDEALL DEVTALVERP NVLVCAFEPQ FLAVPQECLI LTMKANQKYF
PLLDAAGKLT NQFLVVSNIS PEDASLVIEG NERVVRPRLA DAKFFFDQDR KKTLASRVAS
LNKVVYHNKL GTQGERMGRV CDIARAIAEL LEPATQVSDP QGLIQKADTA ARLAKTDLLT
DMVGEFPELQ GIMGGYYALN DGLSTEVAQA IEDHYKPRFA GDALPRNLTG VVVALADKLE
TLVGMFGVGN LPTGDKDPFA LRRHALGVIR MLVEKDLSLR LDELVEAAIP VFGDKIVDPS
LALTDFIFDR LRGYIDLELA YPAPPIEGAD ASAIEKTVAA SYSTNEVDAV LALKPQRLGD
VPKRLAAVRT FAVLPEAPAL AAANKRISNI LKKADAASVA DAHVSALLLK EPAEIALYAV
MQDITPRAQA QCDAGDYAAS LQTLAALRVP VDAFFEDVMV NAEALDMRLN RLGLLKTLHL
AMNQVADLSR LAA
//
