(data stored in ACNUC7421 zone)

SWISSPROT: SYGA_PSEHT

ID   SYGA_PSEHT              Reviewed;         300 AA.
AC   Q3IDE6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 76.
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=PSHAa0005;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954246; CAI85119.1; -; Genomic_DNA.
DR   RefSeq; WP_011326737.1; NC_007481.1.
DR   ProteinModelPortal; Q3IDE6; -.
DR   SMR; Q3IDE6; -.
DR   STRING; 326442.PSHAa0005; -.
DR   EnsemblBacteria; CAI85119; CAI85119; PSHAa0005.
DR   GeneID; 32566071; -.
DR   KEGG; pha:PSHAa0005; -.
DR   eggNOG; ENOG4108HMW; Bacteria.
DR   eggNOG; COG0752; LUCA.
DR   HOGENOM; HOG000264291; -.
DR   KO; K01878; -.
DR   OMA; LGSYYQF; -.
DR   OrthoDB; POG091H01SB; -.
DR   Proteomes; UP000006843; Chromosome I.
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; Q3IDE6.
DR   SWISS-2DPAGE; Q3IDE6.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    300       Glycine--tRNA ligase alpha subunit.
FT                                /FTId=PRO_1000047471.
SQ   SEQUENCE   300 AA;  34122 MW;  9AFB90B90E581E71 CRC64;
     MQKYDVKTFQ GLILALQDYW AQQGCVIIQP LDMEVGAGTF HPQTFLKSIG PEPMSSAYVQ
     PCRRPTDGRY GENPNRLQHY YQFQVVLKPS PDNIQELYLG SLAAVGIDTL TDEVRFVEDN
     WESPTLGAWG LGWEIWLNGM EVTQFTYFQQ VGGIECSPVT GEITYGLERL AMYIQGVDSI
     YDLVWADGPL GRVTYGDVFH QNEVEQSTYN FEHANVEDLF AQFDKCEAES QKLIEANLPL
     PAYEQVMKAS HAFNLLDARH AISVTERQRY ILRVRALSKA CAQSYYDKRE ALGFPLCKDK
//

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