ID A0A3D8MXN8_9DELT Unreviewed; 696 AA.
AC A0A3D8MXN8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=DV096_10635 {ECO:0000313|EMBL:RDV38259.1};
OS Bradymonadaceae bacterium TMQ3.
OC Bacteria; Deltaproteobacteria; Bradymonadales; Bradymonadaceae.
OX NCBI_TaxID=2283320 {ECO:0000313|EMBL:RDV38259.1, ECO:0000313|Proteomes:UP000256871};
RN [1] {ECO:0000313|EMBL:RDV38259.1, ECO:0000313|Proteomes:UP000256871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMQ3 {ECO:0000313|EMBL:RDV38259.1,
RC ECO:0000313|Proteomes:UP000256871};
RA Wang S.;
RT "Lujinxingia celare sp. nov., isolated from a marine island.";
RL Submitted (AUG-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|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:RDV38259.1}.
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DR EMBL; QRGZ01000003; RDV38259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8MXN8; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000256871; 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 SMART; SM00836; DALR_1; 1.
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 589..694
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 696 AA; 75325 MW; 86986EEF386B7FAE CRC64;
MEFIFEIGCE ELPARFVPAA LDQLRDLFTE AAADARLTHG AIRTMGTPRR LTLLIDELSE
AQADLSEERT GPPLKAAYRD GQPTKAAEGF ARGQGVTLED LYTVETDKGE YIAAKVFEKG
QPATEILPAL LEGILAKLNF PKSMRWADLS LSFARPVRWI VAVAGGELVK MSFAGVQSQA
QTYGHRFAAP GAIDVASISG YLNDLRAADV EPDPAARKAT IEVALKEHAE AIGARVIDDP
ELVEEVTYLV EKPFAVTLPF SEAYLELPPE VLISSMRSHQ RYFALENPDG SGLMAACVII
YNTPVRDPEL VAKGNLRVLK ARLDDARFFW DRDLKTPLAD RVAELERVVW LAKIGTMKER
TERIGELAGR VGKTLGLEGQ SLDDAARAGL LSKADLVTQL VFEFTDLQGV MGRAYAQKSG
ENEAVAQAIY DQYLPKGADE ELPGSEVGAS VAIAEKLDAI VGCFGIGLVP SSNADPYGLR
RAALGVIRIL DAAGYNVTLD QLIDQAIATY QAKNPGVLND DTASLAGAVK AFLVTRLDYL
LRDAAPTDVV NAVLAAGVTD IPSVRGRVKA LASLRDQADF EPLAIGFKRV VNILAKQAAE
LDEAPPTNPE LFEEDAEKAL FDAFSTTRQT VEAALATSDW QKACDALIGL KSPVDRFFDD
VMVMTDDTAL RQNRLALLSG LRDLFFGVAD ISKIQA
//
