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Database: UniProt
Entry: I1ZJJ6_STRPA
LinkDB: I1ZJJ6_STRPA
Original site: I1ZJJ6_STRPA 
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}.
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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
//
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