ID   SYGB_SYNY3              Reviewed;         722 AA.
AC   Q55690;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Glycine--tRNA ligase beta subunit;
DE            EC=6.1.1.14;
DE   AltName: Full=Glycyl-tRNA synthetase beta subunit;
DE            Short=GlyRS;
GN   Name=glyS; OrderedLocusNames=slr0220;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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;
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; BA000022; BAA10219.1; -; Genomic_DNA.
DR   PIR; S76367; S76367.
DR   AlphaFoldDB; Q55690; -.
DR   SMR; Q55690; -.
DR   IntAct; Q55690; 1.
DR   STRING; 1148.1001591; -.
DR   PaxDb; Q55690; -.
DR   EnsemblBacteria; BAA10219; BAA10219; BAA10219.
DR   KEGG; syn:slr0220; -.
DR   eggNOG; COG0751; Bacteria.
DR   InParanoid; Q55690; -.
DR   OMA; LPIPKRM; -.
DR   PhylomeDB; Q55690; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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   PANTHER; PTHR30075; PTHR30075; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
DR   TIGRFAMs; TIGR00211; glyS; 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..722
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_0000072933"
SQ   SEQUENCE   722 AA;  80051 MW;  F7085BA5A23436D7 CRC64;
     MPLQTFLFEI GTEELPADFV RSAITQWQGL IPPGLAAEFL QPESVEIYGT PRRLAVLIKG
     LPECQPDRLE EIKGPPASAA FKDGQPTPAA LGFAKKQGVN PEDFEIRSTP KGDFIFVNKQ
     LQGQASRDLL PKLALSWLKA LDGRRFMRWG DGDWRFPRPI RWLVCLLDDQ VLPLQIDNGS
     TTLVGDRLSR GHRILHPADV SLEHGQNYLA QLKTAGVVVD PQERRAMIEQ QITTQAATLE
     GEAIIYEDLL DEVEQLVEYP TAVLGKFDQE FLSLPREVTT TVMVTHQRYF PVVDKDGRLL
     PHFITIANGD PSKGDIIAAG NGRVIRARLA DAKFFYQADC DDSLDSYLPQ LETVTFQEEL
     GTMRDKVDRI MEMAAAIADQ LGVTEQQRGE IDSTAMLCKA DLVTQMVYEF PELQGIMGEK
     YALVSGESAA VAQGIVEHYL PRHQDDDLPQ GLPGQVVGMA DRLDTLVSIF GLGLLPTGSS
     DPFALRRAAN AVINVAWAAS LEINLLELLT QGCRDFVTSH PDKTSPLQAL KTFFLQRLQT
     LLQDEQGIDY DLVNAVLGNG ETNCDEAQSR LHDRLLADLQ DVKERAQYLQ ELRDNGHLDA
     IYPTVNRSAK LASKGTLPTD QLDPRPVIQA PQLVQDSEKA VYQALLAIYP KAVEVQESRD
     YETLVNALHE LAPTVAEFFD GPDSVLVMAE NDELRQNRLN LLGLIRNYAL ILGDFGAIVK
     GI