UniProt: A0A1G8LQU0

Database: UniProt
Entry: A0A1G8LQU0_9PSED

LinkDB:  A0A1G8LQU0_9PSED 
Original site:  A0A1G8LQU0_9PSED

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (7)   
   InterPro (3)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (15)   

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ID   A0A1G8LQU0_9PSED        Unreviewed;       684 AA.
AC   A0A1G8LQU0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE            EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00255};
DE   AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE            Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00255};
GN   Name=glyS {ECO:0000256|HAMAP-Rule:MF_00255};
GN   ORFNames=SAMN05216272_11234 {ECO:0000313|EMBL:SDI58072.1};
OS   Pseudomonas panipatensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=428992 {ECO:0000313|EMBL:SDI58072.1, ECO:0000313|Proteomes:UP000199636};
RN   [1] {ECO:0000313|EMBL:SDI58072.1, ECO:0000313|Proteomes:UP000199636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 7469 {ECO:0000313|EMBL:SDI58072.1,
RC   ECO:0000313|Proteomes:UP000199636};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC         EC=6.1.1.14; Evidence={ECO:0000256|ARBA:ARBA00000201,
CC         ECO:0000256|HAMAP-Rule:MF_00255};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00255}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00255}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00255}.
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DR   EMBL; FNDS01000012; SDI58072.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8LQU0; -.
DR   STRING; 428992.SAMN05216272_11234; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000199636; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
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:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   NCBIfam; TIGR00211; glyS; 1.
DR   PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00255};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00255}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00255};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00255};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00255}.
FT   DOMAIN          580..683
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
SQ   SEQUENCE   684 AA;  73692 MW;  9CC41BD3B10B9874 CRC64;
     MSAKDFLVEL GTEELPPKAL KSLGEAFLAG IEKGLKSAGL SYSAARYYAA PRRLAVQIDG
     LAAQQPDRTV NLDGPPLQAA FDVNGNPTQA ALGFAKKCGV DLAQIDKSGP KLKFSQSIAG
     QPAVSLLPAI VETSLNELPI PKRMRWAARR EEFVRPTQWL VMLFGDDVVE CEILTQKAGR
     ESRGHRFHNP DQVRISSPAN YLEDLRSAHV LADFAERREL IAKRVAELAA EQKGSAIVPA
     DLLDEVTALV EWPVPLVCSF EERFLAVPQE ALITTMQDNQ KYFCLLDANG KLLPRFITVA
     NVQSKAPEHI VSGNEKVVRP RLTDAEFFFK QDKKQPLEQF NERLKNVVFQ AQLGTVFDKA
     ERVSALAAFI AERIGGNAQN AARAGILSKC DLATEMVGEF PEMQGIAGYY YATAGGEAND
     VALALNEQYM PRGAGAELPS TLTGAAVAVA DKLDTLVGIF GIGMLPTGSK DPYALRRAAL
     GVLRILIEKQ LDLDLGEAIA VAVGQYGDKV KAEGLAAQVQ DFIFDRLRAR YEDEGVDVAV
     YQAVRALTPT APLDFDQRVQ AVQAFRQLAE AETLAAANKR VSNILAKAEG EVPASVNDSL
     LNEAAEKALG SAVAAAASEV APLAAARDYR AALARLAALR APVDAFFEEV LVNADDSAVR
     ANRYALLAQL RGLFLGVADI SLLG
//

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