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Database: UniProt
Entry: U4UMY2_DENPD
LinkDB: U4UMY2_DENPD
Original site: U4UMY2_DENPD 
ID   U4UMY2_DENPD            Unreviewed;       751 AA.
AC   U4UMY2;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   08-NOV-2023, entry version 29.
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=D910_08856 {ECO:0000313|EMBL:ERL91526.1};
OS   Dendroctonus ponderosae (Mountain pine beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Dendroctonus.
OX   NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL91526.1, ECO:0000313|Proteomes:UP000030742};
RN   [1] {ECO:0000313|EMBL:ERL91526.1, ECO:0000313|Proteomes:UP000030742}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA   Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA   Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA   Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA   Birol I., Jones S.J., Bohlmann J.;
RT   "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT   a major forest pest.";
RL   Genome Biol. 14:R27-R27(2013).
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; KB632288; ERL91526.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4UMY2; -.
DR   STRING; 77166.U4UMY2; -.
DR   Proteomes; UP000030742; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          76..132
FT                   /note="WHEP-TRS"
FT                   /evidence="ECO:0000259|PROSITE:PS51185"
FT   DOMAIN          313..631
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   751 AA;  84565 MW;  B7F4FA0BCE5B3D80 CRC64;
     MKVAYAILRH LVKFKFVNNP LKHTGAQVVQ ARNLSASPYL NQEYNQKTDW GKNKKGRKVK
     LNLYFDTMGD PQIEQVLAPL RASVKEQGDL VRQLKADGAP ELDVKKAVLE LKARKKILED
     KELALAPNAT FDRAKMEDLL KRRFFYDQSF AIYGGISGQF DFGPMGCAFK SNLLNLWRQS
     FVFEEQMLEV SCSILTPEQV LKASGHVDRF ADLMVKDVKS GECFRLDHLI KAHLEKIAAD
     KKATVETKEE CTDIVIKVSS TLILDGMNKE EMAAILQKFQ MKSPTTGNDL TEPIEFNLMF
     GTQIGPSGLA KGYLRPETAQ GIFVNFKRLL EFNQGKLPFA VAQIGDSFRN EISPRSGLIR
     VREFTMAEIE HFCDPNDKNH PKFEDVKDVE LLLYSACNQM DGKAAERKTI GAAVSTGLVA
     NETLGYFIAR IQQFMVKSGV DPKRLRFRQH MANEMAHYAC DCWDAECLTS YGWIECVGCA
     DRSAFDLTQH SKASGVRLAA EKKLDQPKTV DVVEAAPNKG ALGKEFKKDA KKIQDTLASL
     SIQDIEAIEK NLDSSGTYEL NAGDQKFKLT KNHVSVKRYQ KTVHVEDIIP NVIEPSFGIG
     RVMYAIFEHN FKQRENDEQR TYLSLPAVVA PLKCSVLPLS SNSEFKPIIK QLSTDLTKVV
     VSHTVDDSSG SIGRRYARTD EIAIPYGITI DFDTLKEPHT VTLRERDSMT QVRIPLTEIA
     DVVHNLAYNK QSWTVVQNKY PKFEQQESKG N
//
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