ID A0A0M0LPR4_9EUKA Unreviewed; 593 AA.
AC A0A0M0LPR4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=glycine--tRNA ligase {ECO:0000256|ARBA:ARBA00012829};
DE EC=6.1.1.14 {ECO:0000256|ARBA:ARBA00012829};
DE AltName: Full=Diadenosine tetraphosphate synthetase {ECO:0000256|ARBA:ARBA00030057};
GN ORFNames=Ctob_012101 {ECO:0000313|EMBL:KOO52976.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO52976.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00008226}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOO52976.1}.
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DR EMBL; JWZX01000433; KOO52976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0LPR4; -.
DR OrthoDB; 5476000at2759; -.
DR Proteomes; UP000037460; Unassembled WGS sequence.
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 Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR HAMAP; MF_00253_B; Gly_tRNA_synth_B; 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; IPR022961; Gly_tRNA_ligase_bac.
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:SF8; DNA POLYMERASE SUBUNIT GAMMA-2, MITOCHONDRIAL; 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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:KOO52976.1}; 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:UP000037460};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 103..497
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 57..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 65464 MW; A3CD39AAFFB96855 CRC64;
MCTLLGSAQI AAQGNVVREL KTALKDGKAE KAAVDAAVGV LVALKAKLPA EAAVAAPKSK
KETKAAAPAA APTAAPTAAP AAPTASAPAT VGGDGGLAVS IDDVINVCKR RGIIFQSSEV
YGGYAGFWDY GPLGVELRAN IKQAWWRDMV HRRDDVVGLD SSIIGSPKIW KASGHIDGFS
DPMVDCRTSK LRFRADQLFW SRAEVDGQLL GYVSLLETDD MDELVLEAAT KLQRKAGLRG
TLSCTPVKDF TEASDEEQSL VPSPATGEAG SLTPPRAFNL MFQTNVGAMV DQSSVAYLRP
ETAQGIFTNF KNVVATGRVK VPFGIAQIGK AFRNEITPRN FIFRSREFEQ MEIEYFIDDQ
DATWPVEHER WLQTMWNWLK SIGLREDLMA RDVHESHKLA HYARACTDIM FTFPFGTQEL
MGCAARGNFD LTQHAAASGK SMEYFDDETK AKYVPHVIEP SIGVDRLMLA VLCSAYAEDE
VGGEKRSVLK LHPRLAPIKA AVLPLVKNKP ELVEKAQAIY KRLQRRYYVT YDDSGQIGRR
YRRMDEVGTP YCITVDFETL EDDSVTIRER DSTLQRRIKL PELLEFLEEQ IDA
//
