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Database: UniProt
Entry: A0A0N0U4S8_9HYME
LinkDB: A0A0N0U4S8_9HYME
Original site: A0A0N0U4S8_9HYME 
ID   A0A0N0U4S8_9HYME        Unreviewed;       720 AA.
AC   A0A0N0U4S8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   08-NOV-2023, entry version 23.
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   ORFNames=WN51_01362 {ECO:0000313|EMBL:KOX72994.1};
OS   Melipona quadrifasciata.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Melipona.
OX   NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX72994.1, ECO:0000313|Proteomes:UP000053105};
RN   [1] {ECO:0000313|EMBL:KOX72994.1, ECO:0000313|Proteomes:UP000053105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0111107301 {ECO:0000313|EMBL:KOX72994.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KOX72994.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Melipona quadrifasciata.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ435808; KOX72994.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0U4S8; -.
DR   STRING; 166423.A0A0N0U4S8; -.
DR   OrthoDB; 546660at2759; -.
DR   Proteomes; UP000053105; 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   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   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KOX72994.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          70..126
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
FT   DOMAIN          301..599
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   720 AA;  81921 MW;  C0D0D92C7171552D CRC64;
     MQFVSRNLQL LCKRATRGLY KHNSIYKQLL RRFTVTARLG DFTKWGTTKK NRKVKVQIRQ
     DMSDPKIEDI LAPLRNNVKE QGDYVRKLKS DGAPELDIKK AVVELKLRKK LLEEKELSLS
     ETVEFDRARM DDLLKRRFFF DQSFAIYGGI SGQFDFGPMG CALKTNVLNT WRSFFILEEQ
     MLEVDCSILT PEPVLQASGH VERFADLMVK DIKSGECFRL DHLIKSHLEK VISDKKTNEN
     VSAECKDIII KLDGMTKDEM AAVMSKFNIK SPITGNDLTE PIEFNLMFGT QIGPSGLVKG
     FLRPETAQGI FVNFKRLLAF NQDRLPFAAA QIGNAFRNEI SPRSGLLRVR EFTMAEIEHF
     CDPNDKNHPK FENVKDLSDA VLNKLIANET LGYFMGRIYL FLIKVGIDPK RLRFRQHMGN
     EMAHYACDCW DAECLTSYGW IECVGCADRS AYDLTQHTKA TGVKLVAEKK LSAPKNLDVC
     EVVSNKVIIG KTFKKDSKLV QDALAALNES NINALETEIN ENGETELKLS NGTRVKITKG
     MIEVKRYQKT VHVEEIIPSV IEPSFGIGRI MYAIFEHNFK AREGDEKRTY FSLPPIVAPL
     KCSVLPLSGN SEFIPFVKHL SQNLTSVDVS HKIDDSSGSI GRRYARTDEI AIPFGITIDF
     DTLKTPHTAT LRERDSMGQV RINLDEIPNV VRDLSNGKRT WLEVEQKYPK FEQQETTEVQ
//
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