UniProt: A0A157SAB4

Database: UniProt
Entry: A0A157SAB4_9BORD

LinkDB:  A0A157SAB4_9BORD 
Original site:  A0A157SAB4_9BORD

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (7)   
   InterPro (3)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (18)   

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ID   A0A157SAB4_9BORD        Unreviewed;       712 AA.
AC   A0A157SAB4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
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   ECO:0000313|EMBL:SAI66846.1};
GN   ORFNames=SAMEA3906487_00462 {ECO:0000313|EMBL:SAI66846.1};
OS   Bordetella trematum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=123899 {ECO:0000313|EMBL:SAI66846.1, ECO:0000313|Proteomes:UP000076825};
RN   [1] {ECO:0000313|EMBL:SAI66846.1, ECO:0000313|Proteomes:UP000076825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H044680328 {ECO:0000313|EMBL:SAI66846.1,
RC   ECO:0000313|Proteomes:UP000076825};
RG   Pathogen Informatics;
RL   Submitted (APR-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; LT546645; SAI66846.1; -; Genomic_DNA.
DR   RefSeq; WP_063491503.1; NZ_UFUJ01000001.1.
DR   AlphaFoldDB; A0A157SAB4; -.
DR   STRING; 123899.SAMEA3906487_00462; -.
DR   GeneID; 56588127; -.
DR   KEGG; btrm:SAMEA390648700462; -.
DR   PATRIC; fig|123899.6.peg.445; -.
DR   eggNOG; COG0751; Bacteria.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000076825; Chromosome 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000076825}.
FT   DOMAIN          608..710
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
SQ   SEQUENCE   712 AA;  76761 MW;  C97D6B148435E11E CRC64;
     MTTTIHPLLV ELLTEELPPK ALNRLGQAFA EGVRANLERQ GLLAEDCQST AYATPRRLAV
     RLSAVRAQAP DQPFTEKLMP AKIGLTENGQ ATPALLKKLA AKGLEHLDPA TLERESDGKQ
     DYLIARGTAT GAQLAEGLQD ALEKAIDGLP IPKVMRYQLA DGQTSVKFVR PAHRLVALFG
     ADIVPVSALG LSAGRNTLGH RFMSEGELVI PQADAYEAIL AESGHVIASF EARRAEIERQ
     LQAEANRLSA TLGDDPEVTA LLDEVTALVE HPTVYVGQFE ETFLQVPQEC LILTMRLNQK
     YFPLFDPATG KLTHRFLIVS NMHTGNPANI IEGNQRVVRP RLADAQFFFE TDRKVPLAAR
     VEQLGSIVYH NKLGTQLERV ERVRAIARGV AEALGANVSS CDRAALLAKA DLGSNMVGEF
     PELQGIMGAY YAAGDGEPAD VVEALRSQYR NRCDRPVQPE TLTAAVLFLA ERAETLLGIW
     AIGLAPTGER DPFGLRRAAL GVISAFEQLA AGGWLKISAD GPLSLDGLLQ LAEASFPAGK
     VPTDTRAEVR AFIYERYRNQ LIVEHDRHAV DAVIALAPPL HQVAERVRAV TAFGQLPEAE
     SLAAANKRIG NLLKKAEGDI GDIDAALLAE PAEQALAAAI DALRPQAEAC LAAGDFAGNL
     RTLAQARSAV DAFFADVMVM ADDARVRANR LALLSQLHGL MNQVADISRL AQ
//

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