(data stored in ACNUC7421 zone)

SWISSPROT: C3MHD1_SINFN

ID   C3MHD1_SINFN            Unreviewed;       320 AA.
AC   C3MHD1;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 57.
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:ACP24259.1};
GN   OrderedLocusNames=NGR_c04630 {ECO:0000313|EMBL:ACP24259.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24259.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24259.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate
CC       + glycyl-tRNA(Gly). {ECO:0000256|HAMAP-Rule:MF_00254,
CC       ECO:0000256|SAAS:SAAS00392644}.
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:SAAS00392629}.
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; CP001389; ACP24259.1; -; Genomic_DNA.
DR   RefSeq; WP_012707044.1; NC_012587.1.
DR   RefSeq; YP_002825012.1; NC_012587.1.
DR   STRING; 394.NGR_c04630; -.
DR   EnsemblBacteria; ACP24259; ACP24259; NGR_c04630.
DR   GeneID; 7791689; -.
DR   KEGG; rhi:NGR_c04630; -.
DR   PATRIC; fig|394.7.peg.3271; -.
DR   eggNOG; ENOG4108HMW; Bacteria.
DR   eggNOG; COG0752; LUCA.
DR   HOGENOM; HOG000264291; -.
DR   KO; K01878; -.
DR   OMA; LGSYYQF; -.
DR   OrthoDB; POG091H01SB; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
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; C3MHD1.
DR   SWISS-2DPAGE; C3MHD1.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00104890, ECO:0000313|EMBL:ACP24259.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00514602};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00514628};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00514596, ECO:0000313|EMBL:ACP24259.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00514600};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00514587};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
SQ   SEQUENCE   320 AA;  35796 MW;  33522D6E7A17E72C CRC64;
     MTTASLPDHM NPKRSFQALI LTLHSYWADK GCAVLQPYDM EVGAGTFHPA TTLRALGPKP
     WRAAYVQPSR RPTDGRYGEN PNRLQHYYQY QVLLKPNPSN LQELYLGSLE AIGLDPLLHD
     IRFVEDDWES PTLGAWGLGW ECWCDGMEVS QFTYFQQVCG IECSPVSGEL TYGLERLAMY
     VQGVDNVYDL NFNGREGAEK ITYGDVFLQA EQEYSRHNFE YANTAMLHQH FVDAEKECLA
     LLAAGAPGDA SNNRLHKCVL PAYDQCIKAS HVFNLLDARG VISVTERQSY ILRVRTLAKA
     CGEAFLLTDA GGANETRDAA
//

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