UniProt: A0A192D610

Database: UniProt
Entry: A0A192D610_9SPHN

LinkDB:  A0A192D610_9SPHN 
Original site:  A0A192D610_9SPHN

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (3)   
   Pfam (2)   
   PROSITE (1)   
All databases (16)   

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ID   A0A192D610_9SPHN        Unreviewed;       703 AA.
AC   A0A192D610;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-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   ORFNames=A9D12_11985 {ECO:0000313|EMBL:ANK13535.1};
OS   Erythrobacter neustonensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1112 {ECO:0000313|EMBL:ANK13535.1, ECO:0000313|Proteomes:UP000078263};
RN   [1] {ECO:0000313|EMBL:ANK13535.1, ECO:0000313|Proteomes:UP000078263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9434 {ECO:0000313|EMBL:ANK13535.1,
RC   ECO:0000313|Proteomes:UP000078263};
RA   Shi X.-L., Wu Y.-H., Cheng H., Xu L., Zhang X.-Q., Wang C.-S., Xu X.-W.;
RT   "Compelete Genome Sequence of Bacteriochlorophyll-Synthesizing Bacterium
RT   Porphyrobacter neustonensis DSM 9434.";
RL   Submitted (MAY-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; CP016033; ANK13535.1; -; Genomic_DNA.
DR   RefSeq; WP_068352142.1; NZ_CP016033.1.
DR   AlphaFoldDB; A0A192D610; -.
DR   STRING; 1112.A9D12_11985; -.
DR   KEGG; pns:A9D12_11985; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000078263; 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:UP000078263}.
FT   DOMAIN          616..691
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   703 AA;  75723 MW;  F780F356AAE2B201 CRC64;
     MANFLLELRC EEIPARMQAG ARAELEKLFR RELDAAGVKV GELTIWSTPR RLALIARGLP
     LATEAVSEEA KGPPEGAPDA AIDGFCKKAG VTREQLELRD VKGRMTYFAV IAQPGRAMTD
     VLAAAIPAII RDFSWPKSMR WGAASITTDA LRWVRPLSGI VALLDGAVID VEVGGIRSGA
     TTRGHRFHHD GDITIASTGN YAEKLRAAHV IVDHEERAAI IREGAAKAAA DAGLTLVADE
     GLVIENAGLT EWPVPLLGRF DEDFLDVPPE VIQLTARVNQ KYFVCEDADG KLANAFVCTA
     NIDPSDASVV VDGNRKVLAA RLSDARFFWE QDQKTPLAQH AHKLARITFH EKLGTVADKV
     ERVASLARWL CEQGIVAGDP ALAEQAARLA KADLVTEMVG EFPELQGLMG GYYAAREGLP
     QEVSDAIRDH YKPVGQGDDV PTAPVTVAVS LADKLDTLRS FFAIDEKPTG SKDPFALRRA
     ALAVIRLIAE NDLRLGVAEG DLLDFFADRL KVQQREAGVR HDLIDAVFAL GGEDDLVRLL
     ARVHALQAFV TTEDGANLLA GYKRAANILK KEDWHGIEGE IAATGEEDPL AGVDDPDLAP
     VIAAKMADRH AAASTLSYTP EPAEKALIDA LDTAAPRAAA AVDSERFADA MAALATLRAA
     VDRFFEEVTV NDADAGKRAA RLALLARFRD AVHRVADFSR IEG
//

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