(data stored in ACNUC7421 zone)

SWISSPROT: SYGA_EDWI9

ID   SYGA_EDWI9              Reviewed;         302 AA.
AC   C5B996;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 44.
DE   RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE            EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00254};
DE   AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE            Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00254};
GN   Name=glyQ {ECO:0000255|HAMAP-Rule:MF_00254};
GN   OrderedLocusNames=NT01EI_0015;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate
CC       + glycyl-tRNA(Gly). {ECO:0000255|HAMAP-Rule:MF_00254}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00254}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00254}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00254}.
DR   EMBL; CP001600; ACR67276.1; -; Genomic_DNA.
DR   RefSeq; WP_012846896.1; NC_012779.2.
DR   ProteinModelPortal; C5B996; -.
DR   SMR; C5B996; -.
DR   STRING; 634503.NT01EI_0015; -.
DR   PRIDE; C5B996; -.
DR   EnsemblBacteria; ACR67276; ACR67276; NT01EI_0015.
DR   GeneID; 7959335; -.
DR   KEGG; eic:NT01EI_0015; -.
DR   eggNOG; ENOG4107QIB; Bacteria.
DR   eggNOG; COG0752; LUCA.
DR   HOGENOM; HOG000264291; -.
DR   KO; K01878; -.
DR   OMA; LGSYYQF; -.
DR   OrthoDB; POG091H01SB; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd00733; GlyRS_alpha_core; 1.
DR   HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR   Pfam; PF02091; tRNA-synt_2e; 1.
DR   PRINTS; PR01044; TRNASYNTHGA.
DR   TIGRFAMs; TIGR00388; glyQ; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B996.
DR   SWISS-2DPAGE; C5B996.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    302       Glycine--tRNA ligase alpha subunit.
FT                                /FTId=PRO_1000204588.
SQ   SEQUENCE   302 AA;  34668 MW;  2616B98BB2221C60 CRC64;
     MQKFDIKTFQ GLILTLQDYW ARQGCTIVQP LDMEVGAGTS HPMTCLRALG PEPMATAYVQ
     PSRRPTDGRY GENPNRLQHY YQFQVVIKPS PDNIQELYLG SLKALGLDPT VHDIRFVEDN
     WENPTLGAWG LGWEVWLNGM EVTQFTYFQQ VGGLECKPVT GEITYGLERL AMYIQGVDSV
     YDLVWSDGPL GKTTYGDVFH QNEVEQSTYN FEYADVDFLF ACFEQYEKEA RMLLELEHPL
     PLPAYERILK AAHSFNLLDA RKAISVTERQ RYILRIRTLT KMVAEAYYAS REALGFPMCK
     KD
//

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