(data stored in ACNUC1104 zone)

SWISSPROT: D3UYL6_XENBS

ID   D3UYL6_XENBS            Unreviewed;       302 AA.
AC   D3UYL6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 52.
DE   RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE            EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00254};
DE   AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE            Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00254};
GN   Name=glyQ {ECO:0000256|HAMAP-Rule:MF_00254,
GN   ECO:0000313|EMBL:CBJ79394.1};
GN   OrderedLocusNames=XBJ1_0243 {ECO:0000313|EMBL:CBJ79394.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79394.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79394.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79394.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522,
CC         ChEBI:CHEBI:456215; EC=6.1.1.14; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00254, ECO:0000256|SAAS:SAAS01125800};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00254, ECO:0000256|SAAS:SAAS00514589}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254,
CC       ECO:0000256|SAAS:SAAS00104849}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00254,
CC       ECO:0000256|SAAS:SAAS00578611}.
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DR   EMBL; FN667741; CBJ79394.1; -; Genomic_DNA.
DR   RefSeq; WP_012986856.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0243; -.
DR   EnsemblBacteria; CBJ79394; CBJ79394; XBJ1_0243.
DR   GeneID; 8829866; -.
DR   KEGG; xbo:XBJ1_0243; -.
DR   eggNOG; ENOG4107QIB; Bacteria.
DR   eggNOG; COG0752; LUCA.
DR   HOGENOM; HOG000264291; -.
DR   KO; K01878; -.
DR   OMA; SYYQFQV; -.
DR   BioCyc; XBOV406818:XBJ1_RS01060-MONOMER; -.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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; D3UYL6.
DR   SWISS-2DPAGE; D3UYL6.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00470070, ECO:0000313|EMBL:CBJ79394.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00470125};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00470083};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00514596, ECO:0000313|EMBL:CBJ79394.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00470150};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00470089};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
SQ   SEQUENCE   302 AA;  34443 MW;  4616E0F237547763 CRC64;
     MQKFDTKTFQ GLILTLQDYW ARQGCTIVQP LDMEVGAGTS HPMTCLRALG PEPIAAAYVQ
     PSRRPTDGRY GENPNRLQHY YQFQVIIKPS PDNIQELYLG SLKALGLDPT VHDIRFVEDN
     WENPTLGAWG LGWEVWLNGM EVTQFTYFQQ VGGLECKPVT GEVTYGLERL AMYIQGVDSV
     YDLVWSDGPL GKTTYGDIYH QNEVEQSTYN FEHADVDFLF TCFEQYEKEA QELLALEAPL
     PLPAYERILK AGHTFNLLDA RKAISVTERQ RYILRIRTLT KSVAEAYYAS REALGFPMCK
     KN
//

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