ID A0A369T6J9_9PROT Unreviewed; 723 AA.
AC A0A369T6J9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=DRB17_15665 {ECO:0000313|EMBL:RDD60898.1};
OS Ferruginivarius sediminum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Ferruginivarius.
OX NCBI_TaxID=2661937 {ECO:0000313|EMBL:RDD60898.1, ECO:0000313|Proteomes:UP000253941};
RN [1] {ECO:0000313|EMBL:RDD60898.1, ECO:0000313|Proteomes:UP000253941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WD2A32 {ECO:0000313|EMBL:RDD60898.1,
RC ECO:0000313|Proteomes:UP000253941};
RA Wang S.;
RT "Venubactetium sediminum gen. nov., sp. nov., isolated from a marine solar
RT saltern.";
RL Submitted (JUL-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}.
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:RDD60898.1}.
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DR EMBL; QPMH01000018; RDD60898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369T6J9; -.
DR Proteomes; UP000253941; 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:UP000253941}.
FT DOMAIN 610..715
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
FT REGION 59..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 79426 MW; F93592FC7E57C8FB CRC64;
MAEFLLELFS EEIPARMQAR AAAELKRLAS DKLAEAGLAF DAAESFVTPR RLTLSIIGLP
EKQPDTTEEK KGPKVGAPQK ALDGFLRANG LASADEAEQR ETEKGTFYFV VRHMAGRPTT
EVLAGIVPEL ARGLSWPKSM RWATYGMRYV RPLHGVLALF DGAPIAGELE LGGRTLTFGR
ETRGHRFLAP AAFEVTSTAD YRAKLEKAKV VLDPAERRER IRARAETLAA DEGLRVKDDP
GLLEENVGLA EWPVVLMGRI DAQFMELPPE VLTVSMRTHQ KYFALERADG SLAPRFLLVS
NMETPDGGAA IVAGNERVLR ARLSDAQFFW EQDRKESLVD RVSALQDVVF HARLGSLHHK
VDRMEALAVT IADWIAEANR DKVRSAALLA KADLTTGMVG EFPELQGVMG RYYALADGEA
PEVAEAIADH YAPQGPNDRC PDAPVSVAVS LADKLDTLTG FFTIGEKPTG SKDPFALRRA
ALGVIRLIVE NELRLPLGKV LAEAFHLQPE DAQQAFRSHL AAAAQASDRG VSAAEHVPHA
EEALTGEVLD FLMDRLKVVL RDRGVRHDLI SAIFAVEAPE GGPEDDLVRL LARVEALRAF
LQSDDGANLL TAYRRAGNIV RIEEKKDKAS YRDVDPALFQ DAAEKAVWQN LSAVRETIGK
ALRGETFQDA MTELARLRAP IDDFFEKVMV NTDDRAVRAN RLALLHSIVT VMNQVADFSK
IEG
//
