UniProt: A0A2U8GQ80

Database: UniProt
Entry: A0A2U8GQ80_9RHOO

LinkDB:  A0A2U8GQ80_9RHOO 
Original site:  A0A2U8GQ80_9RHOO

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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   A0A2U8GQ80_9RHOO        Unreviewed;       697 AA.
AC   A0A2U8GQ80;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
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=CEW83_10980 {ECO:0000313|EMBL:AWI75674.1};
OS   Parazoarcus communis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Parazoarcus.
OX   NCBI_TaxID=41977 {ECO:0000313|EMBL:AWI75674.1, ECO:0000313|Proteomes:UP000244930};
RN   [1] {ECO:0000313|EMBL:AWI75674.1, ECO:0000313|Proteomes:UP000244930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSPY31 {ECO:0000313|EMBL:AWI75674.1,
RC   ECO:0000313|Proteomes:UP000244930};
RA   Woo J.-H., Kim H.-S.;
RT   "Azoarcus.";
RL   Submitted (JUN-2017) 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; CP022187; AWI75674.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U8GQ80; -.
DR   KEGG; acom:CEW83_10980; -.
DR   Proteomes; UP000244930; 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:UP000244930}.
FT   DOMAIN          589..688
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   697 AA;  75205 MW;  0489AB22051F9400 CRC64;
     MTSATLLVEL LTEELPPKAL PRLGETFAAK IAEGLKARGL APAAATFRSF ASPRRLAVTV
     ADVVAAAAAK DVTEKLMPVS VALDAEGKPT QALLKKMEAK GIALDAVAGF ERRVDGKAEA
     LFHTATVPGA KLEDVLSTIV QDAVKALPIP KVMRWGDGDA TFVRPVHKLS MLHGADVVPG
     RVLDLDSGRT TRGHRFMSRG EIDIATANAY EPTLLAEGKV MPDFAERRAE IERQLIAEAA
     RQQASIGEYA DLLDEVAALV EHPTVYVGEF EAEFLAVPQE CLILTMRANQ KYFPLFDVDG
     TLLNRFLIVS NMQLEDPSNI VIGNQRVVRP RLSDARFFFE QDKKQTLESR LPRLASVVYH
     NKLGNQFERV ERLGVLAGHI AGLLSADVQA ATRAALLAKV DLVTDMVGEF PELQGVMGRY
     YARHDGESAV VADAIQAHYQ PRFAGDVLPD GNVACAVALA DKLDALVGFF GIGMVPTGDR
     DPFALRRAAL GVLRILMEAP LPLQLPQLIE LAAAGFAPGL LTAEGFQAQL QDFMLERLRN
     LLREGAGGRD AAVADAVLAL RPARIDLVPA KLDAVEAFLA LPESAALAAA NKRIVNILKK
     TEAQPGEPDV ALLQEEAEKA LFHQLNEIAP LVSSHVANEN YTEALLKLAS LRDAVDAFFD
     GVMVMAEEPL TRQNRLALLA RLAGLMNQVA DLSRLSA
//

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