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Database: UniProt
Entry: A0A2K6DXL9_MACNE
LinkDB: A0A2K6DXL9_MACNE
Original site: A0A2K6DXL9_MACNE 
ID   A0A2K6DXL9_MACNE        Unreviewed;       712 AA.
AC   A0A2K6DXL9;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Glycine--tRNA ligase {ECO:0000256|ARBA:ARBA00019404};
DE            EC=6.1.1.14 {ECO:0000256|ARBA:ARBA00012829};
DE   AltName: Full=Diadenosine tetraphosphate synthetase {ECO:0000256|ARBA:ARBA00030057};
GN   Name=GARS1 {ECO:0000313|Ensembl:ENSMNEP00000040661.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000040661.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000040661.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000713};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34936;
CC         Evidence={ECO:0000256|ARBA:ARBA00000713};
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:0000256|ARBA:ARBA00001768};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16014;
CC         Evidence={ECO:0000256|ARBA:ARBA00001768};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226}.
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DR   AlphaFoldDB; A0A2K6DXL9; -.
DR   STRING; 9545.ENSMNEP00000040661; -.
DR   Ensembl; ENSMNET00000065154.1; ENSMNEP00000040661.1; ENSMNEG00000043203.1.
DR   GeneTree; ENSGT00940000153759; -.
DR   OMA; MEMQYFV; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000043203; Expressed in temporal lobe and 12 other cell types or tissues.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004081; F:bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity; IEA:Ensembl.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:Ensembl.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015966; P:diadenosine tetraphosphate biosynthetic process; IEA:Ensembl.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:Ensembl.
DR   CDD; cd00774; GlyRS-like_core; 1.
DR   CDD; cd00858; GlyRS_anticodon; 1.
DR   CDD; cd00935; GlyRS_RNA; 1.
DR   Gene3D; 3.30.40.230; -; 1.
DR   Gene3D; 3.30.720.200; -; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR   Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 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; IPR002315; tRNA-synt_gly.
DR   InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR   InterPro; IPR000738; WHEP-TRS_dom.
DR   NCBIfam; TIGR00389; glyS_dimeric; 2.
DR   PANTHER; PTHR10745:SF0; GLYCINE--TRNA LIGASE; 1.
DR   PANTHER; PTHR10745; GLYCYL-TRNA SYNTHETASE/DNA POLYMERASE SUBUNIT GAMMA-2; 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; SSF52954; Class II aaRS ABD-related; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   PROSITE; PS00762; WHEP_TRS_1; 1.
DR   PROSITE; PS51185; WHEP_TRS_2; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..712
FT                   /note="Glycine--tRNA ligase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014432272"
FT   DOMAIN          62..118
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
FT   DOMAIN          261..581
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   712 AA;  79921 MW;  859243F568D412AD CRC64;
     MPSPRPALLR GARAALLLLL PPRLLARPSL PPRRPLSAPS CAPISFPAAS RSSMDGAGAE
     EVLAPLRLAV RQQGDLVRKL KEDKAPQVDV DKAVAELKAR KRVLEAKELA LQPKDDIVDR
     AKMEDTLKRR FFYDQAFAIY GGVSGLYDFG PVGCALKNNI IQTWRQHFIQ EEQILEIDCT
     MLTPEPVLKT SGHVDKFADF MVKDVKNGEC FRADHLLKAH LQKLMSDKKC SVEKKSEMES
     VLAQLDNYGQ QELTDLFVNY NVKSPITGND LSPPVSFNLM FKTFIGPGGN MPGYLRPETA
     QGIFLNFKRL LEFNQGKLPF AAAQIGNSFR NEISPRSGLI RVREFTMAEI EHFVDPSEKD
     HPKFQNVADL HLYLYSAKAQ VSGQSARKMR LGDAVEQVLP NTKMIMCTLW GSQISVGKDT
     LKSPQHGWIE IVGCADRSCY DLSCHARATK VPLVAEKPLK EPISFLVVQF EPNKGAIGKA
     YKKDAKLVME YLAICDECYI TEMEMLLNEK GEFTIETEGK TFQLTKDMVN VKRFQKTLYV
     EEVVPNVIEP SFGLGRIMYT VFEHTFHVRE GDEQRTFFSF PAVVAPFKCS VLPLSQNQEF
     MPFVKELSEA LTRHGVSHKV DDSSGSIGRR YARTDEIGVA FGVTIDFDTV NKTPHTATLR
     DRDSMRQIRA EVSELPSIVR DLANGSITWA DVEARYPLFE GQETGKKETI EE
//
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