UniProt: A0A0N7LS38

Database: UniProt
Entry: A0A0N7LS38_9RHOB

LinkDB:  A0A0N7LS38_9RHOB 
Original site:  A0A0N7LS38_9RHOB

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

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ID   A0A0N7LS38_9RHOB        Unreviewed;       720 AA.
AC   A0A0N7LS38;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
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:CUH52540.1};
GN   ORFNames=SHM7688_01987 {ECO:0000313|EMBL:CUH52540.1};
OS   Shimia marina.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae.
OX   NCBI_TaxID=321267 {ECO:0000313|EMBL:CUH52540.1, ECO:0000313|Proteomes:UP000054823};
RN   [1] {ECO:0000313|EMBL:CUH52540.1, ECO:0000313|Proteomes:UP000054823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7688 {ECO:0000313|EMBL:CUH52540.1,
RC   ECO:0000313|Proteomes:UP000054823};
RG   Swine Surveillance;
RL   Submitted (SEP-2015) 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; CYPW01000018; CUH52540.1; -; Genomic_DNA.
DR   RefSeq; WP_058239759.1; NZ_FOMU01000010.1.
DR   AlphaFoldDB; A0A0N7LS38; -.
DR   STRING; 321267.SHM7688_01987; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000054823; Unassembled WGS sequence.
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:UP000054823}.
FT   DOMAIN          608..712
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   720 AA;  78619 MW;  9515E2C49D47910C CRC64;
     MPDLLIELFS EEIPARMQAR AAEDLKKKVT DGLVEAGLTY AHARAYSTPR RLTLALEGLL
     AESPTVNEER KGPKVGAPDK AIEGFLRGAG VAREDLEERE TPKGAVYFAT ITKPGRPAAE
     IVAEVLEDTI RNFPWPKSMR WGAGSLRWVR PLHSILCILS AEDGHSIVPL DIDGITSGDT
     TEGHRFMGEG RFAVTSFEDY EVKLKRSKVV LNAEERAETI WNDATNMAFA QGLEVVEDKG
     LLAEVAGLVE WPVVLMGDIA EDFLGLPPEV LQTSMKEHQK FFSVKNPKTG RIEKFVTVAN
     RATKDDGATI LAGNQKVLFA RLSDAKFFWE NDVRTVQDQG FEPWVEKLDN VTFHAQIGSQ
     GARVMRIAHL ASVLAPSVNA DPMLAQMAAQ ACKADLSSEM VYEFPELQGL MGRYYAQAAE
     LPVEVGQASE EHYSPLGPSD DVPSAPVSVA VAMADKLDTL SGFWAIDEKP TGSKDPYALR
     RAALGVIRLV LENGLRINLL ETTATAVAAL LKVDEWDAAA QDAEGDDAKH MAMQAAQARG
     IVEAAPGDLL SFFHDRLKVY LRDQGIRHDV IDACIAMPGN DDLALLVARA RALQDFMSTE
     DGENLLQGFK RANNILSQAE EKDGVEYSYG ADVKFAEDDS EKTLFAVLDQ AEGAISSAIE
     AEDFASAMGT MASLRAPIDA FFEAVQVNSD NDVVRRNRLN LLSRIRTICL QAADLTRVEG
//

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