ID A0A1I7TWM9_9PELO Unreviewed; 754 AA.
AC A0A1I7TWM9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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};
OS Caenorhabditis tropicalis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold629.g12525.t2};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold629.g12525.t2}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) 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; A0A1I7TWM9; -.
DR STRING; 1561998.A0A1I7TWM9; -.
DR WBParaSite; Csp11.Scaffold629.g12525.t2; Csp11.Scaffold629.g12525.t2; Csp11.Scaffold629.g12525.
DR eggNOG; KOG2298; Eukaryota.
DR Proteomes; UP000095282; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro.
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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 77..133
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 134..632
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 754 AA; 85904 MW; 6378962FC136A735 CRC64;
MHCKKIHEII VFIEGSIKAP RFSFGSSLTA LVEVVAGNRN AAQSQVKKVQ APRFEKKTRQ
KISDYLKQMA TPEIEAQLAP LRAAVKEYGD LIRDLKAKSA PKIDIDKAVV ELKARKRLLE
ETEISLAPKE ASFDRLKLED LLKRRFFYDQ SFAIYGGVTG LYDFGPMGCS LKANMLQEWR
KHFILEEGML EVDCTSLTPE PVLKASGHVD RFADWMVKDV KNGECFRADH LIKNSIEKLM
NDKKVSADVK RDGEDVLARL EGFDDKDMHE VITRFKFKSP ITGNDLTEPI AFNLMFPTQI
GPTGDFKAFL RPETAQGIFV NFKRLLEFNQ GKLPFAAAQI GLGFRNEISP RQGLIRVREF
TMCEIEHFVD PEDKSFPKFS KIADQKLVLF PHVINWMEHQ RRKSPSEMLL QTKMTIYIMF
QKTVANETLG YYMARCHQFL MKVGIDGRRL RFRQHLSNEM AHYAQDCWDA EILTSYGWIE
CVGNADRACY DLLQHYKATN VKLVAEKKLP QPVDVDIVEA QANMALLGKS FKKEAKKIQS
ALQQMTSEQV TSLEADLLSK KLFNLNINGE AYPLTPDLIN IKKYSKKIHV QEITPSVIEP
SYGIGRIMYA LLEHSFRQRE GDEQRTFLAF KPLVAPIKCS VLPISANDQL VAGIEAVKEE
LSRYELSYKV DDSSGTIGRR YARTDEIGIP FGITVDFESV KTTPYTVTIR HAETMSQIRL
EVSELGRLIS DLVAGRQQWT DAQAKYPKFE STTD
//
