UniProt: A0A1G9D0G7

Database: UniProt
Entry: A0A1G9D0G7_9RHOB

LinkDB:  A0A1G9D0G7_9RHOB 
Original site:  A0A1G9D0G7_9RHOB

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (7)   
   InterPro (3)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (15)   

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ID   A0A1G9D0G7_9RHOB        Unreviewed;       687 AA.
AC   A0A1G9D0G7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=SAMN05216257_103302 {ECO:0000313|EMBL:SDK57412.1};
OS   Meinhardsimonia xiamenensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Meinhardsimonia.
OX   NCBI_TaxID=990712 {ECO:0000313|EMBL:SDK57412.1, ECO:0000313|Proteomes:UP000199328};
RN   [1] {ECO:0000313|Proteomes:UP000199328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10789 {ECO:0000313|Proteomes:UP000199328};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FNFV01000003; SDK57412.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9D0G7; -.
DR   STRING; 990712.SAMN05216257_103302; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000199328; 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   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:UP000199328}.
FT   DOMAIN          578..685
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
SQ   SEQUENCE   687 AA;  75765 MW;  539B19B5D0E133D2 CRC64;
     MPDLLIELFS EEIPARMQAR AAGDLERLMV SGLREAGLVC RGARAFATPR RLALAVEGLP
     KESPARREER KGPRVDAPEQ ALEGFLRSTG LTRDQLEARE DKKGNKVWFA VIERPGRPAA
     EIVAEVLGEV IRSFPWPKSM RWGSGSLRWV RPLHAILAIL HDEAGAQVVP FEIEGIRAGD
     STRGHRFMAP EPFSVTSFDD YVAKLKRAKV ILDPVERADI ILQEAESAAF AQGLELVHDK
     GLLAEVAGLV EWPVVLMGAI GEEFLGLPPE VLQTSMREHQ KFFSVRNPKT GRIERFVTVA
     NIEAADGGAT ILAGNAKVLA ARLSDARFFW ENDLRRVREE GMVGMAEGLK AVTFHARLGS
     QWDRVQRIRR LAREIAPVVG AKPDLADEAA EICKADLVSE MVYEFPELQG IMGRYYAKSA
     GHDDGVPEAC EEHYKPLGAS DDVPSAPVSI AVALADKIDT LTGFWAIGEK PTGSKDPFAL
     RRAALGVIRI VLENGLRLRL QELFAHGYPG ADAGDLLAFF HDRLKVHLRE QGIRHDIIDA
     CLAMPGNDDL TLVVKRAQAL ADMLATEDGE NLLQGFRRAN NILTQAEERD GVEYSFGADP
     KFAEHPAEKA LFSALDEAEE KIAPAMERED FEAAMQAMAA LRGPIDAFFE AVQVNTDNEI
     VRRNRLNLLS RIRTLCLSVA DLRRIEG
//

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