UniProt: A0A2S0MJA7

Database: UniProt
Entry: A0A2S0MJA7_9BURK

LinkDB:  A0A2S0MJA7_9BURK 
Original site:  A0A2S0MJA7_9BURK

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

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ID   A0A2S0MJA7_9BURK        Unreviewed;       752 AA.
AC   A0A2S0MJA7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, 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=C6570_04215 {ECO:0000313|EMBL:AVO35969.1};
OS   Ottowia oryzae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ottowia.
OX   NCBI_TaxID=2109914 {ECO:0000313|EMBL:AVO35969.1, ECO:0000313|Proteomes:UP000239709};
RN   [1] {ECO:0000313|EMBL:AVO35969.1, ECO:0000313|Proteomes:UP000239709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KADR8-3 {ECO:0000313|EMBL:AVO35969.1,
RC   ECO:0000313|Proteomes:UP000239709};
RA   Kim S.-J., Heo J., Kwon S.-W.;
RT   "Genome sequencing of Ottowia sp.";
RL   Submitted (MAR-2018) 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; CP027666; AVO35969.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S0MJA7; -.
DR   KEGG; otk:C6570_04215; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000239709; Chromosome.
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   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}; Reference proteome {ECO:0000313|Proteomes:UP000239709}.
FT   DOMAIN          641..743
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   752 AA;  80331 MW;  4546C8A7BE33E420 CRC64;
     MNTSQNLLVE LFVEELPPKA LKKLGDAFAS QLAEQLKSQG LLAADAVVTP YASPRRLAAH
     VTQVAAKAAD KAVQQKLMPV TVGLDAAGNA TPALLKKLQA LGADASVVPQ LKRAPDGKAE
     ALFLDTVVPG ATLAAGLQKA LHEAIAKLPI PKVMTYQLEQ NTPLPGWDSV QFVRPAHGLV
     ALHGADVVPV TALGLTAGRA AHGHRFEAKA APIELANADA YAATLRDEGA VIASFDERRA
     AIESQLKAAA AQAGPALAAI KDEALLDEVT ALVERPNVLT CAFDKAFLDV PQECLILTMK
     ANQKYFPLLD AAGKLTHQFL VVSNISPADA SAVIEGNERV VRPRLADAKF FFDQDRKKTL
     ESRVDGLAKV VYHNKLGTQG ERVERVRAIA RAIGQQLGGD VLAKSADDAA KLAKADLLTD
     MVGEFPELQG IMGGYYARHD GWSEDIAFAI EDHYKPRFAG DDLPRGQTGT VVALADKLET
     LVGMFGIGNL PTGDKDPFAL RRHALGVIRL IVEKGLPLGL RELITNVYEI FNDVALQEAY
     HSKRAESVVA EGLQQQRRDG ISGIQTVGYG HSLIKLDPAT PAKVEAFAFD RLAGLLREQS
     YSTQDVDAVL AMQPQRLVEV PHRLKAVRAF AELPEAPALA AANKRIGNIL KKAEPDGALQ
     AAVNADLLQE PAEQALYTAL QQTVPQADAQ FAAGDYTGSL KTLAALRAPV DAFFDGVMVN
     AEDPALKANR LALLQQLHQA MNRVADLSRL AA
//

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