SYGA_GLOVI
ID SYGA_GLOVI Reviewed; 290 AA.
AC Q7NKN1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00254};
DE AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00254};
GN Name=glyQ {ECO:0000255|HAMAP-Rule:MF_00254}; OrderedLocusNames=glr1446;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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:0000255|HAMAP-Rule:MF_00254};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00254}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00254}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00254}.
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DR EMBL; BA000045; BAC89387.1; -; Genomic_DNA.
DR RefSeq; NP_924392.1; NC_005125.1.
DR RefSeq; WP_011141446.1; NC_005125.1.
DR AlphaFoldDB; Q7NKN1; -.
DR SMR; Q7NKN1; -.
DR STRING; 251221.35212011; -.
DR EnsemblBacteria; BAC89387; BAC89387; BAC89387.
DR KEGG; gvi:glr1446; -.
DR PATRIC; fig|251221.4.peg.1478; -.
DR eggNOG; COG0752; Bacteria.
DR HOGENOM; CLU_057066_1_0_3; -.
DR InParanoid; Q7NKN1; -.
DR OMA; SYYQFQV; -.
DR OrthoDB; 676868at2; -.
DR PhylomeDB; Q7NKN1; -.
DR Proteomes; UP000000557; 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:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00733; GlyRS_alpha_core; 1.
DR Gene3D; 3.30.930.10; -; 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 Pfam; PF02091; tRNA-synt_2e; 1.
DR PRINTS; PR01044; TRNASYNTHGA.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00388; glyQ; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..290
FT /note="Glycine--tRNA ligase alpha subunit"
FT /id="PRO_1000047426"
SQ SEQUENCE 290 AA; 33562 MW; 166AAA87060609BF CRC64;
MNFQDMTLSL HRFWEEQGCL IVQPYDVEKG AGTMNPHTFL RAIGPEPWNV AYIEPCRRPT
DGRYAQNPNR LQHYYQYQVL MKPSPGDIQE RYLRSLEVLG IHPEKHDVRF VEDNWESPTL
GAWGVGWEVW LDGMEVTQFT YFQQCGGIDC RPVSIEITYG IERLAMYLQG VDSIFDIEWG
AGLTYGQVHR EGEIENCIYN FEQANPELLF TLFKLYEQEA TALSERRLVL PALDYVLKCS
HTFNLLDARG VIAVTERTGY IGRIRHLARR IAQAYAKQRE SLGFPLLSKT