ID A0A1A9T335_9PROT Unreviewed; 697 AA.
AC A0A1A9T335;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=A7981_02755 {ECO:0000313|EMBL:OAM52419.1};
OS Methylovorus sp. MM2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylovorus.
OX NCBI_TaxID=1848038 {ECO:0000313|EMBL:OAM52419.1, ECO:0000313|Proteomes:UP000077545};
RN [1] {ECO:0000313|Proteomes:UP000077545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM1 {ECO:0000313|Proteomes:UP000077545};
RA Macey M.C., Murrell J.C.;
RT "Draft genome of Methylovorus sp. MM1 isolated from grassland soil.";
RL Submitted (MAY-2016) 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:OAM52419.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LXUF01000001; OAM52419.1; -; Genomic_DNA.
DR RefSeq; WP_067263696.1; NZ_LXUF01000001.1.
DR AlphaFoldDB; A0A1A9T335; -.
DR STRING; 1848038.A7981_02755; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000077545; 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}; Reference proteome {ECO:0000313|Proteomes:UP000077545}.
FT DOMAIN 592..695
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 697 AA; 75649 MW; A1B993CB03804B24 CRC64;
MSTKNLLVEL FVEELPPKAL KKLGEAFSFV LFEALKSQGL TTDDSQVTAY ASPRRLAAHI
TQVPAQAADK ALSQKLMPVT VGFDAAGNPS PALLKRLAAL GADESAIPKL KRESDGKAES
LFLDIVQTGA QLAEGLQRAL DETLAKLPIP KVMTYQLADG WSNVNFVRPA HGLVALHGSD
VVAINILGLQ ASNTTHGHRF EAKVDTIILK DADSYSEQLK IEGAVIASFD ERRDEIVRQL
NAAAAKENLK PIDDDALLDE VAALVERPNI LLGQFETEYL EVPQECLILT MKANQKYFPL
LDANNKLTNK FLIVSNISPA DPSAVIGGNE RVVRPRLADA KFFFDQDRKK TLESRVASLD
KVVYHNKLGS QGERNQRVRA IAKSIGQQLG GNHLAAKADQ AAQLSKADLL TDMVGEFPEL
QGIMGGYYAR HDGLDHEVAD AIEDHYKPRF SGDDLPRNQV GIVVALADKL ETLIGLFSIG
ERPTGDKDPF ALRRHALGII RLLIENKLPL TLTGLIQDSA ATVSLGIPVE LETFFYDRLA
VNLREQGYSA QEVDAVLSLK PELLADITKR LEAVRAFATL PEAESLAAAN KRVGNILKKS
ETAVTAQIDA SLLQEAAEKS LAAALSNVQP LADKAFESGD YTGSLQALAA LKTPVDDFFD
HVMVNAEDPK LKANRLGLLA TLYQAMNRIA DLSKLAS
//
