ID A0A243PDR9_9SPHN Unreviewed; 749 AA.
AC A0A243PDR9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-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 ORFNames=CA262_06810 {ECO:0000313|EMBL:OUC54598.1};
OS Sphingobium sp. GW456-12-10-14-TSB1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1987165 {ECO:0000313|EMBL:OUC54598.1, ECO:0000313|Proteomes:UP000194660};
RN [1] {ECO:0000313|EMBL:OUC54598.1, ECO:0000313|Proteomes:UP000194660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW456-12-10-14-TSB1 {ECO:0000313|EMBL:OUC54598.1};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-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:OUC54598.1}.
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DR EMBL; NGUN01000003; OUC54598.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A243PDR9; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000194660; 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; 2.
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 650..739
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
FT REGION 378..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 749 AA; 80811 MW; 4C43167FB60D59CA CRC64;
MTDFLLELRC EEIPARMQLK ASDDLARLFS EELAKSGLTP GAIDSFVTPR RLALIARDLP
LETAAVSEEH KGPRTSAPPQ ALEGFLRKTG LTQDQLEDRD GVWFAVINKP GRATADVLAQ
AIPAIIRAFP WPKSMRWGSA SQTTESLRWV RPLQAIVAIL GEDLIPCEVD GIQSGYATLG
HRFHHSGEIT IGGASDYAEK LRACHVIVSH QERQSIIAEK SAQAAAAHGY TVVEDKGLIA
ENAGLTEWPV PLLGDFDPAF LEVPPEVIQL TLRINQKYFV LRDGQGKLAP AFICTANIEA
KDGGAAIIAG NRKVLAARLS DARFFWEQDR KTRLEDHAKK LERITFHEKL GTVADKVERV
ANLARWLVEE GIVTPTTPAT TVTPAKAGVS GGSTPTPEMP ASTGMTKEQL AQLAYDAAML
CKADLVTEMV GEFPELQGIM GGYYARAEGL PDAVADAIRD HYKPVGQGDD VPTAPVTVAV
SLADKLDTIG SFFAIGERPT GSKDPFALRR AALGLISSAV ENNVRFPLEK LFIAALAEKQ
RTADGDPEAV FHLFDFFIER LKVQQRTAGV RHDLIEAVFM AEEETEVLRL LARVHALQSF
VATDDGANLL AGYKRAANIL KKEAPAQPTT VIPAKAGTHL PTEQSDTAAA MDSRLRGNDG
PLSYTPEIAE AALIAALDVA EPRTAQAVAA EDFEGAMAAL ATLRAPIDAF FESVTVNDPD
ADKRAARLAL LARVRDAVHS VADFSKITG
//
