ID A0A1I8C6X3_9BILA Unreviewed; 737 AA.
AC A0A1I8C6X3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 08-NOV-2023, entry version 26.
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 Rhabditophanes sp. KR3021.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC Rhabditophanes.
OX NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000093500.1};
RN [1] {ECO:0000313|WBParaSite:RSKR_0000093500.1}
RP IDENTIFICATION.
RC STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000093500.1};
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; A0A1I8C6X3; -.
DR WBParaSite; RSKR_0000093500.1; RSKR_0000093500.1; RSKR_0000093500.
DR Proteomes; UP000095286; 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 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 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 Coiled coil {ECO:0000256|SAM:Coils};
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 73..129
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 264..615
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT COILED 74..121
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 737 AA; 83240 MW; D12A0B0478316052 CRC64;
MISSFARLLS RNYNNLRVLR SLSSPFYKVP VAASAKVTHR KSLQGDQIYT KKFKQRLSDY
LKTAMNAPEI EARLAALRSD LKETADIVRQ LKANNAPKID IDQQVTLLKA KKKKLEDAEI
DLMPKDAAFD RPKLDDLLKR RFFYDQSFAI YGGVSGLYDY GPMGCALKQN MIQMWRNHFI
IKDAMLEVEC SMLTPAPVFV ASGHVERFID WMVRDVKTGE CFRADHLIKN SIEKLKTDKK
TSAQTKEEFE KILDLLDGYD EKDMQRIITQ YGFKSPITGN DLTEPSSFNL MFPTEIGPTG
DFKAYLRPET AQGIFINFKR LLEFNAGKLP FASAQIGPGF RNEISPRQGL IRVREFTMCE
IEHFVDPELK ETPKFKSVAG VVLNLFSADA QMDGKGAVRM AIGDAVKSKL VDNETLGYYM
ARTHLYMIKV GIDETKLRFR QHMSNEMAHY AKDCWDAEVL TSYGWIECAG SCYDLTQHSK
ATNVKLVAEK KLDAPKTISG FEVVPQKAVI GKVYKTQAKD ILAKLAALSV QEIEEVEAKL
KGDQEYTLAS GTGPIKLTNE MITVRPFEKT IHVEEIVPSV IEPSFGIGRI MYAVLEHSFR
TREGDANRNF LELKPSVAPI KCSILPISSN ERFAPLMDLV SHLLSTYGLT FRIDDSAGSI
GRRYARTDEI GIPFGVTVDF ESEKEPHTVT LRHASSTEQV RLEVASVGEI VHKLCSDQLT
WDDVKKQYPL FVTEKEN
//
