GARS_CAEEL
ID GARS_CAEEL Reviewed; 742 AA.
AC Q10039;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Glycine--tRNA ligase;
DE EC=6.1.1.14 {ECO:0000250|UniProtKB:P41250};
DE AltName: Full=Diadenosine tetraphosphate synthetase;
DE Short=Ap4A synthetase;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:P41250};
DE AltName: Full=Glycyl-tRNA synthetase;
DE Short=GlyRS;
GN Name=gars-1 {ECO:0000303|PubMed:22579749, ECO:0000312|WormBase:T10F2.1a};
GN Synonyms=grs-1 {ECO:0000312|WormBase:T10F2.1a};
GN ORFNames=T10F2.1 {ECO:0000312|WormBase:T10F2.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DISRUPTION PHENOTYPE.
RX PubMed=22579749; DOI=10.1016/j.jprot.2012.04.038;
RA Tohsato Y., Monobe K., Suzuki K., Hayano T., Kawasaki I., Ito M.;
RT "Comparative proteomic analysis reveals differentially expressed proteins
RT in Caenorhabditis elegans pgl-1 mutants grown at 20 degrees C and 25
RT degrees C.";
RL J. Proteomics 75:4792-4801(2012).
CC -!- FUNCTION: Catalyzes the ATP-dependent ligation of glycine to the 3'-end
CC of its cognate tRNA, via the formation of an aminoacyl-adenylate
CC intermediate (Gly-AMP). Also produces diadenosine tetraphosphate
CC (Ap4A), a universal pleiotropic signaling molecule needed for cell
CC regulation pathways, by direct condensation of 2 ATPs. Thereby, may
CC play a special role in Ap4A homeostasis.
CC {ECO:0000250|UniProtKB:P41250}.
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:0000250|UniProtKB:P41250};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16014;
CC Evidence={ECO:0000250|UniProtKB:P41250};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H(+) = diphosphate + P(1),P(4)-bis(5'-adenosyl)
CC tetraphosphate; Xref=Rhea:RHEA:34935, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58141;
CC Evidence={ECO:0000250|UniProtKB:P41250};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34936;
CC Evidence={ECO:0000250|UniProtKB:P41250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P41250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41250}. Cell
CC projection, axon {ECO:0000250|UniProtKB:P41250}. Secreted
CC {ECO:0000250|UniProtKB:Q9CZD3}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:Q9CZD3}. Note=Secreted by motor neuron, possibly
CC through the exosome pathway. {ECO:0000250|UniProtKB:Q9CZD3}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in larval
CC lethality. RNAi-mediated knockdown in the germline results in 100%
CC sterility at 25 degrees Celsius. {ECO:0000269|PubMed:22579749}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; FO081619; CCD72865.1; -; Genomic_DNA.
DR RefSeq; NP_498093.1; NM_065692.3.
DR AlphaFoldDB; Q10039; -.
DR SMR; Q10039; -.
DR BioGRID; 40934; 10.
DR IntAct; Q10039; 1.
DR STRING; 6239.T10F2.1a; -.
DR EPD; Q10039; -.
DR PaxDb; Q10039; -.
DR PeptideAtlas; Q10039; -.
DR EnsemblMetazoa; T10F2.1a.1; T10F2.1a.1; WBGene00001744.
DR GeneID; 175703; -.
DR KEGG; cel:CELE_T10F2.1; -.
DR UCSC; T10F2.1b.1; c. elegans.
DR CTD; 175703; -.
DR WormBase; T10F2.1a; CE29472; WBGene00001744; gars-1.
DR eggNOG; KOG2298; Eukaryota.
DR InParanoid; Q10039; -.
DR OMA; EPSYGID; -.
DR OrthoDB; 1183820at2759; -.
DR PhylomeDB; Q10039; -.
DR SignaLink; Q10039; -.
DR PRO; PR:Q10039; -.
DR Proteomes; UP000001940; Chromosome III.
DR ExpressionAtlas; Q10039; baseline and differential.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015966; P:diadenosine tetraphosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0070150; P:mitochondrial glycyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00774; GlyRS-like_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR027031; Gly-tRNA_synthase/POLG2.
DR InterPro; IPR033731; GlyRS-like_core.
DR InterPro; IPR009068; S15_NS1_RNA-bd.
DR InterPro; IPR002315; tRNA-synt_gly.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR PANTHER; PTHR10745; PTHR10745; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF00458; WHEP-TRS; 1.
DR PRINTS; PR01043; TRNASYNTHGLY.
DR SMART; SM00991; WHEP-TRS; 1.
DR SUPFAM; SSF47060; SSF47060; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00389; glyS_dimeric; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS00762; WHEP_TRS_1; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cell projection; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Secreted;
KW Transferase.
FT CHAIN 1..742
FT /note="Glycine--tRNA ligase"
FT /id="PRO_0000073002"
FT DOMAIN 73..129
FT /note="WHEP-TRS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00531"
FT BINDING 309
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 341..343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 352..353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 360
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 467..468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 586..588
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250|UniProtKB:P41250"
FT BINDING 593
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P41250"
SQ SEQUENCE 742 AA; 84150 MW; 8FAC5C407AB4F2B7 CRC64;
MFSSCWLKSS VRYSRLIRQF SSENSFFKVE LVPSDRKTPL QPRKVVAPRF EKKTRQKISD
YLKQMATPEI EAKLAPLRAA VKEYGDLIRD LKAKGAPKID IDKAVVELKA RKRLLEDTEI
ALAPKEASFD RLKLEDLLKR RFFYDQSFAI YGGVTGLYDF GPMGCSLKAN MLQEWRKHFI
LEEGMLEVDC TSLTPEPVLK ASGHVDRFAD WMVKDMKNGE CFRADHLIKN SIEKLLNDKK
TSAAVKQDGQ DVLARLEGFD NKDMHEVITR FNFKSPITGN DLTEPIAFNL MFPTQIGPTG
DFKAFLRPET AQGIFVNFKR LLEFNQGKLP FAAAQIGLGF RNEISPRQGL IRVREFTMCE
IEHFVDPEDK SLAKFAKVAD QKLVLFSACN QLDGAPAQEV AIGEAVAKKT VANETLGYYM
ARCHQFLMKV GIDGRRLRFR QHLSNEMAHY AQDCWDAEIL TSYGWIECVG NADRACYDLQ
QHYKATNVKL VAEKKLPEPV DVNFVEAQAN MALLGKSFKK DAKKIQTSLQ QLTSEQVSAL
EEELLAKKLY NLSVDGQNYA LTPEHLNIKK YTKKIHVQEI TPSVIEPSYG IGRIMYALLE
HSFRQREGDE QRTFLAFKPL VAPIKCSVLP ISANDTLIPV MDAVKEELSR FEMSYKVDDS
SGTIGRRYAR TDEIGIPFGI TVDFDSLKTT PFTVTIRHAE TMSQIRLEVS ELGRLISDLV
AGRQQWSDAQ AKYPKFEASA TE
