SYGB_GLOC7
ID SYGB_GLOC7 Reviewed; 717 AA.
AC B7KD52;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00255};
DE AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00255};
GN Name=glyS {ECO:0000255|HAMAP-Rule:MF_00255};
GN OrderedLocusNames=PCC7424_4816;
OS Gloeothece citriformis (strain PCC 7424) (Cyanothece sp. (strain PCC
OS 7424)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Gloeothece; Gloeothece citriformis.
OX NCBI_TaxID=65393;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7424;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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_00255};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00255}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00255}.
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DR EMBL; CP001291; ACK73173.1; -; Genomic_DNA.
DR RefSeq; WP_015956755.1; NC_011729.1.
DR AlphaFoldDB; B7KD52; -.
DR SMR; B7KD52; -.
DR STRING; 65393.PCC7424_4816; -.
DR EnsemblBacteria; ACK73173; ACK73173; PCC7424_4816.
DR KEGG; cyc:PCC7424_4816; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_3; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000002384; Chromosome.
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 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..717
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000197173"
SQ SEQUENCE 717 AA; 80555 MW; 248C45A44A1EF7FC CRC64;
MPSFLLEVGT EELPANFVDE AIAQWQSRIP SSLEEQQLTP EGIEFYGTPR RLAVLIKGLP
AKQSDRIEEV KGPAANVAFK SGKPTKALEG FVRKQGVTPD EVEIRDTDKG EFVFVQKNIT
GRNTTEILQE LVPQWITQLE GRRFMRWGDG DLRFPRPIRW LVTLWDQDIL PLELVNGATQ
VKSDRLTYGH RILAPESVSI PEASAYQKSL QQAYVEVSPL QRRQTIEQQI EKVAKQLKGV
AVIPPDLLDE VVNLVEYPSA VAGNFEPDFL NLPTEVITTV MVTHQRYFPV KATGKTNKNN
TLLPYFITIS NGDPNKGEII AAGNERVIRA RLADAQFFYK ADCDEPLESY LPQLETVTFQ
EQLGTIRDKV DRIMEISQLI ADQLDLDSGE RSEIESTAML CKADLVTQMV YEFPELQGVM
GQKYALASGE SPNVALGIFE HYLPRGADDI MPESLTGQVV GLADRIDTIV SIFGLGMIPT
GSGDPFALRR AATGIIKVTW YAELPIDILD LLEQSSQDFV TAHPDKTSPI ESLKSFFIQR
LSTLLQDDLH IDYDLVNAVL GENDPEYTER ALRDLLDVRD RAQFLQSIRN NQKIDEIYET
VNRSARLAVK GELDTQELDP EKVIRPALFE KSSEEHFYKV LIDLVPTTLT AQRERNYQLL
VDALGKIAPT VSNFFDGEDS VLVMDENLEV RENRLNLLGL LRNHARVLAD FGAIVKS