ID A0A0N4Z3T2_PARTI Unreviewed; 425 AA.
AC A0A0N4Z3T2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=glycine--tRNA ligase {ECO:0000256|ARBA:ARBA00012829};
DE EC=6.1.1.14 {ECO:0000256|ARBA:ARBA00012829};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000157500.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0000157500.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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:ARBA00000201};
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
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DR AlphaFoldDB; A0A0N4Z3T2; -.
DR STRING; 131310.A0A0N4Z3T2; -.
DR WBParaSite; PTRK_0000157500.1; PTRK_0000157500.1; PTRK_0000157500.
DR Proteomes; UP000038045; 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:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02091; tRNA-synt_2e; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 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}.
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..368
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 45237 MW; 5EBE7C168973D830 CRC64;
MMSGVGAAAH ALPRPADRQN LQPRRLGQAD QAVEVFGRAA VGGGRALDVM TIGDQPAGRL
GRAGDQRLKV VVGQAAGLQA DGLKVGPVGA SGVDPVAHAA HVAEGPGEGG HDVAVQPLAH
PFGVARQLVR QFGGAQAQGA DVVEGVAADL VPGLMRGLQV FDLELGLADV RAAAQAARDV
IGRPDPVFSQ DRPRLGPGAG WEIIEAEAEN AAGRRDRHRP DAQVARRPAA HLINPLLHHG
RLLAHRRLQK GEGLRRLALL AKRGGPMVRA SRNRTEMSTV AAAEPLSFQD LILTLHHYWS
DQGCAIMQPY DIEVGAGTLH PATVLRALGH PEAEPRQPAG AVSQQPARHR HRPQPARHPL
RRGRLGEPHR RRLGAGLGGL VRRHGGDAVH LFPGRRRHRG RRRLGRADLR AGASGHVCSG
RRQRL
//
