ID A0A452EXW8_CAPHI Unreviewed; 836 AA.
AC A0A452EXW8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:ENSCHIP00000016825.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000016825.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000016825.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000016825.1}
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 EMBL; LWLT01000003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452EXW8; -.
DR STRING; 9925.ENSCHIP00000016825; -.
DR Ensembl; ENSCHIT00000024634.1; ENSCHIP00000016825.1; ENSCHIG00000016912.1.
DR GeneTree; ENSGT00940000153759; -.
DR Proteomes; UP000291000; Chromosome 4.
DR Bgee; ENSCHIG00000016912; Expressed in skin of neck and 18 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; 1.
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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
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:UP000291000};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 160..216
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 359..606
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 836 AA; 93669 MW; 71C4C017016C5DDD CRC64;
MSTNALCKSV RRGSTWGPTA LLYARGGSSP FGALIDCGSF RGFVSNRPVA TRRRVAGWGV
CGCARRGVYA AISSCSRPGR ARRFRRRPLP TSQRRRLMPS LRPALLRAAR AALLQSLPAG
LPARPPLLPC RPISKPARAP TWFPAAASRS SMDGAGAEEV LAPLRLAVRQ QGDLVRKLKE
DKAPQVDIDK AVSELKARKR ILEAKELALQ PKDDVVDRAK MEDTLKRRFF YDQAFAIYGG
VSGLYDFGPV GCALKNNIIQ TWRQHFIQEE QILEIDCTML TPEPVLKTSG HVDKFADFMV
KDLKNGECFR ADHLLKAHLQ KLMSDKKCSA EKKSEMESVL AQLDNYGQQE LADLFVNYNV
KSPTTGNDLS PPVPFNLMFK TFIGPGGNMP GYLRPETAQG IFLNFKRLLE FNQGKLPFAA
AQIGNSFRNE ISPRSGLIRV REFTMAEIEH FVDPSEKDHP KFQNVADIYL YLYSAKAQVS
GQSARKMRLG DAVEQGVINN SVLGYFIGRI YLYLVKVGVS PEKLRFRQHM ENEMAHYACD
CWDAESKTSY GWIEIVGCAD RSCYDLSCHA RATKVPLVAE KPLKEPKTVS VVQFEPNKGA
IGKAYKKDAK LVMEYLAICD ECYITEMEKL LNEKGEFTVE TEGKTFQLTK DMVNVKRFQK
TLHVEEVIPS VIEPSFGLGR IMYTVFEHTF QVREGDEQRT FFSFPAVVAP FKCSVLPLSQ
NQEFMPFVKE LSEALTRHGI SHKVDDSSGS IGRRYARTDE IGVAFGITID FDTVNKTPHT
ATLRDRDSMR QIRAEVSELP GVVRDLANGS IMWADVEARY PVFEGQETGK KEAVEE
//
