(data stored in ACNUC7421 zone)

SWISSPROT: C6B2Q7_RHILS

ID   C6B2Q7_RHILS            Unreviewed;       311 AA.
AC   C6B2Q7;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   05-JUL-2017, entry version 54.
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   OrderedLocusNames=Rleg_0573 {ECO:0000313|EMBL:ACS54877.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54877.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54877.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54877.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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; CP001622; ACS54877.1; -; Genomic_DNA.
DR   EnsemblBacteria; ACS54877; ACS54877; Rleg_0573.
DR   KEGG; rlg:Rleg_0573; -.
DR   HOGENOM; HOG000264291; -.
DR   KO; K01878; -.
DR   OMA; LGSYYQF; -.
DR   OrthoDB; POG091H01SB; -.
DR   Proteomes; UP000002256; 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; C6B2Q7.
DR   SWISS-2DPAGE; C6B2Q7.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00104890, ECO:0000313|EMBL:ACS54877.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00514602};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
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:ACS54877.1};
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}.
SQ   SEQUENCE   311 AA;  34995 MW;  CCDDD035C78A8255 CRC64;
     MNPKRSFQAL ILTLHNYWAD KGCAVLQPYD MEVGAGTFHP ATTLRALGPK PWKAAYVQPS
     RRPSDGRYGE NPNRLQHYYQ YQVILKPNPP NLQELYLGSL AAIGLDPLLH DIRFVEDDWE
     SPTLGAWGLG WECWCDGMEV SQFTYFQQVC GIECSPVAGE LTYGLERLAM YVQGVDNVYD
     LNFNGRDGDE KISYGDVFLQ AEQEYSRHNF EFANTEMLHR HFVDAEKECR ALLDAGAPGD
     NANQRLHKCV FPAYDQCIKA SHVFNLLDAR GVISVTERQS YILRVRTLAK ACGEAFLLTD
     AGGVNLSKEA A
//

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