ID SYGC_ARATH Reviewed; 463 AA.
AC Q9FXG2; F4I358;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 24-JAN-2024, entry version 135.
DE RecName: Full=Putative glycine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.14;
DE AltName: Full=Diadenosine tetraphosphate synthetase;
DE Short=AP-4-A synthetase;
DE AltName: Full=Glycyl-tRNA synthetase;
DE Short=GlyRS;
GN OrderedLocusNames=At1g29870; ORFNames=F1N18.9;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly). Is also
CC able produce diadenosine tetraphosphate (Ap4A), a universal pleiotropic
CC signaling molecule needed for cell regulation pathways, by direct
CC condensation of 2 ATPs (By similarity). {ECO:0000250}.
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: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG10609.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC008030; AAG10609.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31144.1; -; Genomic_DNA.
DR PIR; C86422; C86422.
DR RefSeq; NP_174280.2; NM_102727.2.
DR AlphaFoldDB; Q9FXG2; -.
DR SMR; Q9FXG2; -.
DR BioGRID; 25100; 9.
DR STRING; 3702.Q9FXG2; -.
DR iPTMnet; Q9FXG2; -.
DR PaxDb; 3702-AT1G29870-1; -.
DR ProteomicsDB; 233020; -.
DR EnsemblPlants; AT1G29870.1; AT1G29870.1; AT1G29870.
DR GeneID; 839865; -.
DR Gramene; AT1G29870.1; AT1G29870.1; AT1G29870.
DR KEGG; ath:AT1G29870; -.
DR Araport; AT1G29870; -.
DR TAIR; AT1G29870; -.
DR eggNOG; KOG2298; Eukaryota.
DR HOGENOM; CLU_015515_4_0_1; -.
DR InParanoid; Q9FXG2; -.
DR OMA; GHVKKFT; -.
DR OrthoDB; 681997at2759; -.
DR PRO; PR:Q9FXG2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FXG2; baseline and differential.
DR Genevisible; Q9FXG2; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0015966; P:diadenosine tetraphosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00774; GlyRS-like_core; 1.
DR Gene3D; 3.30.40.230; -; 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; IPR027031; Gly-tRNA_synthase/POLG2.
DR InterPro; IPR033731; GlyRS-like_core.
DR InterPro; IPR002315; tRNA-synt_gly.
DR NCBIfam; TIGR00389; glyS_dimeric; 1.
DR PANTHER; PTHR10745:SF0; GLYCINE--TRNA LIGASE; 1.
DR PANTHER; PTHR10745; GLYCYL-TRNA SYNTHETASE/DNA POLYMERASE SUBUNIT GAMMA-2; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01043; TRNASYNTHGLY.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..463
FT /note="Putative glycine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000073003"
FT REGION 25..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 271..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 281..286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 286..290
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 398..399
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 463 AA; 52168 MW; C5C309379D5A9E66 CRC64;
MDAPEQSFLR EKSLAVEDQE LAVGTLEDSH AAKPETNAAI ELPNKSKPEK SAVEKDREDF
REAVVKTLDR LLFVHKSFDI YHGVAGLYDF GPHGRTVELN ILSLWRKCFV DEEDMMEVAC
TALTPEAVFN ASGHVKKFTD LMVKDEVDGA FHRADHLVKS YCENRKKDPT ISAENAAELD
KVIAHVEDLS AEELGGVWNH CSTAPVTKNP LSHPPRPFNL MFQTSFGASG SLIGYLRPET
AQGSFCNFKD YYNLNGRKLP FAVAQVGRVF RNEISPRQGL LRTREFTLAE IEHFVHPEHK
SHSKFSDVAK LELLMFPREE QEKPGQFAKR LCLGEAVAKG HVNSETLGFF IGRVYLFLIR
LGIDKERLRF RHHLANEMAH YATDCWDAEI ECSYGWIECV GIADRSDYDL RAHSEKSGHA
LVAQEKLAEP IEVEKLAITP EMKELGPAFK GNQKNVVEAL EVD
//
