ID A0A059BDR3_EUCGR Unreviewed; 778 AA.
AC A0A059BDR3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=EUGRSUZ_G01975 {ECO:0000313|EMBL:KCW64347.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW64347.1};
RN [1] {ECO:0000313|EMBL:KCW64347.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW64347.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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; KK198759; KCW64347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059BDR3; -.
DR STRING; 71139.A0A059BDR3; -.
DR EnsemblPlants; KCW64347; KCW64347; EUGRSUZ_G01975.
DR Gramene; KCW64347; KCW64347; EUGRSUZ_G01975.
DR InParanoid; A0A059BDR3; -.
DR OMA; MEMQYFV; -.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004820; F:glycine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0070150; P:mitochondrial glycyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00774; GlyRS-like_core; 1.
DR CDD; cd00858; GlyRS_anticodon; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 97..153
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 166..645
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 85903 MW; 8E945EBB796FF25E CRC64;
MGLHHHLVND RIAATGGRKL STHHPPSKTL ASDIFPSSSV VAERTQICMP PPPSSSPPSL
LARLASSASL ASRLSISRLF SSSPAAMDPT EDSLRKALAG RQAAVDAQGN AVRALKAGKA
PKPEIDAAIK ALNDLKIEKA DVEKRLQAAV SGGAGDGALT REAFRHAVVN TLERRLFYIP
SFKIYRGVAG LYDYGPPGCA VKSNILAYWR QHFVHEENML EVDCPCVTPE IVLKASGHVD
KFTDLMVKDE KTGTCYRADH LLKDFCNEKL QKDLSISAEK AAELKLVLAT LDDLSADKLG
AKIKEYGITA PDTKNPLSDP YPFNLMFQTS IGPSGMLPGY MRPETAQGIF VNFKDLYYYN
GNKLPFAAAQ IGQAFRNEIS PRQGLLRVRE FTLAEIEHFV DPEDKSHPKF SEVADLEFLM
FPREQQMSGQ SAIITRLGEA VSKGTVNNAT LGYFIGRVYL FLTHLGIDKG RLRFRQHLAN
EMAHYAADCW DAEIECSYGW IECVGIADRS AFDLRAHTVR KSGVALVAHE KFAEPREVEK
LVIVPNKKEL GLAFKGNQKM VVESLEAMGE EEAFQLKAAL ESKGEAEFLV CAMGKSVIIK
DNMVNISKQK IRENQRVFTP SVIEPSFGIG RIIYCLFEHS FYTRPNKAGD EQFNVFRFPP
LVAPIKCTVF PLIQKPEYES VAQLISRSLT VAGVSHKIDI TGNTIGKRYA RTDELGVPFA
ITVDSQVDVT IRERDSKDQV RVSVGEVASV VMEVIDGHRT WSDVWSSFPH HTSASAED
//
