UniProt: A0A222E8R8

Database: UniProt
Entry: A0A222E8R8_9RHOB

LinkDB:  A0A222E8R8_9RHOB 
Original site:  A0A222E8R8_9RHOB

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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   A0A222E8R8_9RHOB        Unreviewed;       700 AA.
AC   A0A222E8R8;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
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:ASP22609.1};
GN   ORFNames=ANTHELSMS3_03999 {ECO:0000313|EMBL:ASP22609.1};
OS   Antarctobacter heliothermus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Antarctobacter.
OX   NCBI_TaxID=74033 {ECO:0000313|EMBL:ASP22609.1, ECO:0000313|Proteomes:UP000203589};
RN   [1] {ECO:0000313|EMBL:ASP22609.1, ECO:0000313|Proteomes:UP000203589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS3 {ECO:0000313|EMBL:ASP22609.1,
RC   ECO:0000313|Proteomes:UP000203589};
RA   Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Godhe A.,
RA   Clarke A.K.;
RT   "Genome Sequence of Antarctobacter heliothermus Strain SMS3 Isolated from a
RT   culture of the Diatom Skeletonema marinoi.";
RL   Submitted (JUL-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; CP022540; ASP22609.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A222E8R8; -.
DR   KEGG; aht:ANTHELSMS3_03999; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000203589; 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:UP000203589}.
FT   DOMAIN          589..694
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   700 AA;  76258 MW;  5B3D95F593E05688 CRC64;
     MPDLLIELFS EEIPARMQPK AAEDLKKLMT DGLVEAGLTY EGAQAFSTPR RLALTVHGLT
     GQSPTLREER RGPKVGAPDK ALEGFMRGAG VTRDQLEERT EKKGSFYYAT VTTPGRPAAQ
     IVADVLEQTV RGFPWPKSMR WGTGSLRWVR PLHRIMCLLT DEAGDHPVAL NIDGIPVGQT
     TEGHRFMADG TFDVTSFEDY ETRLKRAHVI LSAQDRADTI WHDATNMAFA QGMEVVEDPG
     LLREVAGLVE WPVVLMGDIG AAFLDLPPEV LQTSMKEHQK FFSVKNPSTG RIEKFITVAN
     IETADNGTTI LAGNQKVLAA RLSDAKFFWE NDLRVAKGAG LSAWTERLGN VTFHNKLGSQ
     RDRIARITGL AREIAPMVGA DAGLAAQAAD VAKADLNSEM VYEFPELQGL MGRYYAQAAG
     LDASVAAACE DHYAPLGPSD DVPDAPVSVA VALADKLDTL TGFWAIDEKP TGSKDPFALR
     RAALGVIRLV LENGLRIDLA TVIRKADFLV AENEDGVIGP SPDVYIPDLI SFIHDRLKVH
     LRAEGIRHDV IDACLAMDGR HDLALVVKRA QALSGFLATE DGGNLLSGFK RANNILTQAE
     DKDGVEYSFG ADVKFAEVEE ERALFTALQA AETRIAPAMA AEEFETAMAA MADLRAPIDA
     FFEAVQVNAD NQIVRRNRLN MLGSIRKTCL QVADLTKIEG
//

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