ID A0A1F2UJU3_9BACT Unreviewed; 700 AA.
AC A0A1F2UJU3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=A3J28_13880 {ECO:0000313|EMBL:OFW31265.1};
OS Acidobacteria bacterium RIFCSPLOWO2_12_FULL_60_22.
OC Bacteria; Acidobacteriota.
OX NCBI_TaxID=1797188 {ECO:0000313|EMBL:OFW31265.1, ECO:0000313|Proteomes:UP000178255};
RN [1] {ECO:0000313|EMBL:OFW31265.1, ECO:0000313|Proteomes:UP000178255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OFW31265.1}.
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DR EMBL; MEKZ01000325; OFW31265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F2UJU3; -.
DR Proteomes; UP000178255; 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}.
FT DOMAIN 579..689
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 700 AA; 77979 MW; E0B9A80E057AD347 CRC64;
MIEGGLADLK RLLEEGFERF RLFGEPRASL EMYGTPRRLI AYCPRLLVRQ ASSVETMQGP
PQRVAFDAQG KPTAAATSFA AKMGTKIEKL ETVSTPKGEY LVFRKQNPGR PTPEILAEMI
PLAVLGISFP RSMYWEGKAG PRFIRPIRSL LALYGGKVVP CSIGAVKAAS WTFGHRLLGK
PRLPVRDFAG YREALRNNYV LIDPQERRAR ILDGVRDLLP SDDGLRLKPN EELLNTLVYL
TEYPTPLLGE FDPAFLALPE EVLITVMKGH QKYLSLEQAD GALAPRFVAV LDRDADPAGA
IRHGHERVLR ARFNDARFFW ETDGKTGLEK RLQALRQVTF QSQLGSYFEK ADRMRRLAAA
FATRLGRAEK LEDIQVAARL AKCDLTTQLV KEFTELQGVV GGLSARREGL SDEIATAIYD
HYKPANLESP SPRTLAGAVV SLADRMDTLA GCFGVGLAPS GSKDPLGLRR AANGVIKILV
DHVLRLPLSQ LVEDAAAVYQ DAKASGRIPD WDHAVVLREL RLFLVDRLRY YLRDVRGFAY
DEVNAVLAAG SEDVVDVVER AEAVARVRPT ENFEPLAVAF KRIQNILRQA QAAGFTGGEL
DPSLLEPGPE RQLYERYRTV AELVARQKQE GDYWAALEAI ASLRPDVDRF FDKGGVMVMA
PEENLRQNRL VLLQGLLREF STIADFFEIV TAEEEKRKAP
//
