ID A0A231RTN2_9BACL Unreviewed; 693 AA.
AC A0A231RTN2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=B1A99_01065 {ECO:0000313|EMBL:OXS62483.1};
OS Cohnella sp. CIP 111063.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=1955714 {ECO:0000313|EMBL:OXS62483.1, ECO:0000313|Proteomes:UP000215193};
RN [1] {ECO:0000313|EMBL:OXS62483.1, ECO:0000313|Proteomes:UP000215193}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 111063 {ECO:0000313|EMBL:OXS62483.1,
RC ECO:0000313|Proteomes:UP000215193};
RA Dastager S.G., Neurgaonkar P.S., Dharne M.S.;
RT "Cohnella sp SGD-V74 (T) CIP 111063, whole genome shotgun sequencing
RT project.";
RL Submitted (MAR-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|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:OXS62483.1}.
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DR EMBL; MWSG01000001; OXS62483.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A231RTN2; -.
DR Proteomes; UP000215193; 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:UP000215193}.
FT DOMAIN 588..680
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 693 AA; 76138 MW; 9231CF586F076010 CRC64;
MAKDLLLEIG MEEVPARFVR AAMEQLQEKT VKWLEDSRLA YGEVKAYATP RRLAVLVSGL
ADKQEDVSED VKGPSRKIAY DESGAWSKPA LGFARSQGVE PDSLFLREIG GVEYVFATKS
SLGVETASLL PEALPALVTS LTFPKNMRWG SHELRYVRPI RWLVALHGDQ VVPFEIAGVA
SGNETHGHRF LGHEAVIAEP SSYVEILRAE HVIVDVEERR RAILTGIESL AAERGWTIGI
KEDLLEEVLF LVETPSALSG SFDPSFLDIP QEVLITSMRE HQRYFPVFDG EGRLLPHFVT
VRNGDRTSID VVAKGNEKVL RARLSDAKFF YEEDKKLVIA DALAKLENIV YHEELGTVAD
KVRRVRVVAD KIAAHLRLEP SAAEDIARTA DICKFDLVSQ MVYEFPELQG IMGEDYARLA
GERETVARAI NEHYSPRNAG DKPAASIVGA IVGIADKLDT IAGCFSIGII PTGSQDPYAL
RRQAAGIVNT LLAHELEITL DELFRIALDV HAQRGLKREA YDVAKDMREF FVLRVKNVLS
EQAIRYDVVD AVLGAGAGDV RRTVLRASAL QAATADEAKA IFRPAVEAFN RVCNLAAKAD
SKQVDANLFA DDAESKLYEA WQQAHGQFVK ATAEADLGGA LSALSSLSAP VTAFFEAVMV
MAEDEALRRN RLAILALVAD DVKQFADFSK LAG
//