(data stored in SCRATCH zone)

SWISSPROT: Q500T6_PSEU2

ID   Q500T6_PSEU2            Unreviewed;       335 AA.
AC   Q500T6;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 91.
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=Psyr_0012 {ECO:0000313|EMBL:AAY35086.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35086.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35086.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35086.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY35086.1; -; Genomic_DNA.
DR   RefSeq; WP_003437077.1; NC_007005.1.
DR   RefSeq; YP_233124.1; NC_007005.1.
DR   STRING; 205918.Psyr_0012; -.
DR   EnsemblBacteria; AAY35086; AAY35086; Psyr_0012.
DR   GeneID; 3365487; -.
DR   KEGG; psb:Psyr_0012; -.
DR   PATRIC; fig|205918.7.peg.12; -.
DR   eggNOG; ENOG4108HMW; Bacteria.
DR   eggNOG; COG0752; LUCA.
DR   HOGENOM; HOG000264291; -.
DR   KO; K01878; -.
DR   OMA; SYYQFQV; -.
DR   BioCyc; PSYR205918:G1G4J-12-MONOMER; -.
DR   Proteomes; UP000000426; 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; Q500T6.
DR   SWISS-2DPAGE; Q500T6.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00470070, ECO:0000313|EMBL:AAY35086.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00254,
KW   ECO:0000256|SAAS:SAAS00470125};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
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:AAY35086.1};
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}.
SQ   SEQUENCE   335 AA;  38359 MW;  C1F5C99450473C2F CRC64;
     MRPNRVYSRS LNRSPAQVKF VSQPTPAVRT FQDLILALQQ YWAEQGCVVL QPYDMEVGAG
     TFHTATFLRA VGPETWNAAY VQPSRRPTDG RYGENPNRLQ HYYQFQVILK PNPDNFQELY
     LGSLKHIGLD PLVHDVRFVE DNWESPTLGA WGLGWEIWLN GMEVSQFTYF QQVGGLECYP
     VTGEITYGLE RLAMYQQGVD SVYDLVWADG PFGKVTYGDV FHQNEVEQST YNFEHANVDK
     LFELFDFYES EAARLIELEL PLPGYEMVLK ASHTFNLLDA RRAISVTARQ QYILRVRTLA
     RSVAQAYLQA RARLGFPMAP PDLRDEVLAK LEAAQ
//

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