ID I1ZJJ6_STRPA Unreviewed; 305 AA.
AC I1ZJJ6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00254};
DE AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00254};
GN Name=glyQ {ECO:0000256|HAMAP-Rule:MF_00254,
GN ECO:0000313|EMBL:AFJ25220.1};
GN ORFNames=Spaf_0195 {ECO:0000313|EMBL:AFJ25220.1};
OS Streptococcus parasanguinis FW213.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1114965 {ECO:0000313|EMBL:AFJ25220.1, ECO:0000313|Proteomes:UP000002865};
RN [1] {ECO:0000313|EMBL:AFJ25220.1, ECO:0000313|Proteomes:UP000002865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW213 {ECO:0000313|EMBL:AFJ25220.1,
RC ECO:0000313|Proteomes:UP000002865};
RX PubMed=22529932; DOI=10.1371/journal.pone.0034769;
RA Geng J., Chiu C.H., Tang P., Chen Y., Shieh H.R., Hu S., Chen Y.Y.;
RT "Complete Genome and Transcriptomes of Streptococcus parasanguinis FW213:
RT Phylogenic Relations and Potential Virulence Mechanisms.";
RL PLoS ONE 7:E34769-E34769(2012).
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_00254};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00254}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00254}.
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; CP003122; AFJ25220.1; -; Genomic_DNA.
DR RefSeq; WP_002886077.1; NC_017905.1.
DR AlphaFoldDB; I1ZJJ6; -.
DR STRING; 1114965.Spaf_0195; -.
DR PaxDb; 1114965-Spaf_0195; -.
DR GeneID; 75174861; -.
DR KEGG; scf:Spaf_0195; -.
DR PATRIC; fig|1114965.3.peg.189; -.
DR eggNOG; COG0752; Bacteria.
DR HOGENOM; CLU_057066_1_0_9; -.
DR Proteomes; UP000002865; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0016740; F:transferase activity; IEA:UniProt.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00733; GlyRS_alpha_core; 1.
DR HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR NCBIfam; TIGR00388; glyQ; 1.
DR PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02091; tRNA-synt_2e; 1.
DR PRINTS; PR01044; TRNASYNTHGA.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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_00254};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00254}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00254};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00254};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00254}.
SQ SEQUENCE 305 AA; 34876 MW; EDFDE2F3962E4535 CRC64;
MSKKLTFQEI ILTLQQYWND QGCMLMQAYD NEKGAGTMSP YTFLRAIGPE PWNAAYVEPS
RRPADGRYGE NPNRLYQHHQ FQVVMKPSPS NIQELYLESL EKLGINPLEH DIRFVEDNWE
NPSTGSAGLG WEVWLDGMEI TQFTYFQQVG GLATGPVTSE VTYGLERLAS YIQEVDSVYD
IEWAPGVKYG EIFLQPEYEH SKYSFEVSDQ DMLLENFEKF EKEAGRALEL GLVHPAYDYV
LKCSHTFNLL DARGAVSVTE RAGYIARIRN LARVVAKTFV AERKKLGYPL LDEATRAKLL
AEEEE
//