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Database: UniProt
Entry: A0A317V7Z3_9EURO
LinkDB: A0A317V7Z3_9EURO
Original site: A0A317V7Z3_9EURO 
ID   A0A317V7Z3_9EURO        Unreviewed;       656 AA.
AC   A0A317V7Z3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
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=BO70DRAFT_365471 {ECO:0000313|EMBL:PWY70175.1};
OS   Aspergillus heteromorphus CBS 117.55.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY70175.1, ECO:0000313|Proteomes:UP000247233};
RN   [1] {ECO:0000313|EMBL:PWY70175.1, ECO:0000313|Proteomes:UP000247233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY70175.1,
RC   ECO:0000313|Proteomes:UP000247233};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:PWY70175.1}.
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DR   EMBL; MSFL01000031; PWY70175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317V7Z3; -.
DR   STRING; 1448321.A0A317V7Z3; -.
DR   VEuPathDB; FungiDB:BO70DRAFT_365471; -.
DR   OrthoDB; 546660at2759; -.
DR   Proteomes; UP000247233; 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:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro.
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   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   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   PRINTS; PR01043; TRNASYNTHGLY.
DR   SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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:PWY70175.1}; 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:UP000247233}.
FT   DOMAIN          202..546
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   656 AA;  74265 MW;  96F23C15CFB2D320 CRC64;
     MASLTTKTGQ VVDRLVLDSM LRRRLFYTPS FEIYGGVSGL YDYGPPGCAI LNNIVDLWRK
     HFVLEEDMLE VDCSMLTPHE ILKTSGHVDK FADWMCKDPK TGEIFRADHL VEEVLESRLK
     GDKEARGQKV EVDEEKEAKK KKKVKQTKVV KLDDAVVKEY EEILAQIDNF DGPDLEKIIA
     KYDIRNPATD GNLLPPVAFN LMFQTSIGPS SNMPGYLRPE TAQGQFLNFQ KLLDFNQQSM
     PFASASIGKS FRNEISPRAG LLRVREFLMA EIEHFVDPEG GKKHSRFAEV KDVEMTLLNR
     HVQLSGSTQT EQMTIGKAVE TGLVDNETLG YFLARIQLFL TKLGVDPKRL RFRQHMANEM
     AHYATDCWDA ELQTSYGWIE CVGCADRSAY DLTVHKNKTG AALVVRETRA EPLKVEEWQI
     DLDKKKFGPR FKKDGKTVTA AIEALSQELR EKLSLDLEQT GKIEVAVEGV PSGKVELDKE
     LIKIEKRTRV ENVREYTPNV IEPSFGIGRI LYSMIEQVYW TREGDEARGV LSFPPAIAPT
     KVLIVPLSTH QSFAPLVQRL TTKLRRMGVS NRVDDSSASI GKRYARNDEL GTPFGVTVDF
     QSVKDDTFTL RDRDSTKQVR ASEDEIAQAI KALVEGEETW EDVRKRLPEF TGQEVE
//
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