UniProt: A0A1H2R3L0

Database: UniProt
Entry: A0A1H2R3L0_9BACL

LinkDB:  A0A1H2R3L0_9BACL 
Original site:  A0A1H2R3L0_9BACL

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (3)   
   Pfam (2)   
   PROSITE (1)   
All databases (14)   

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ID   A0A1H2R3L0_9BACL        Unreviewed;       696 AA.
AC   A0A1H2R3L0;
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=SAMN05444487_101372 {ECO:0000313|EMBL:SDW13941.1};
OS   Marininema mesophilum.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Marininema.
OX   NCBI_TaxID=1048340 {ECO:0000313|EMBL:SDW13941.1, ECO:0000313|Proteomes:UP000198534};
RN   [1] {ECO:0000313|EMBL:SDW13941.1, ECO:0000313|Proteomes:UP000198534}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45610 {ECO:0000313|EMBL:SDW13941.1,
RC   ECO:0000313|Proteomes:UP000198534};
RA   de Groot N.N.;
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|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; FNNQ01000001; SDW13941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2R3L0; -.
DR   STRING; 1048340.SAMN05444487_101372; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000198534; 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:UP000198534}.
FT   DOMAIN          590..680
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   696 AA;  77987 MW;  2C77F901BF5B6CC2 CRC64;
     MPNRDWLLEI GVEEMPARFV PDSLTQLEEK MLHWLDENHI AHGVAETFAT PRRLTIRVRD
     VVEGQADVEE EVRGPAKRIA VGADGGWSKA AVGFARKQGL TTADLVLEEY KGETYVFARR
     HVKGRATVEL LKEGVPEVLS ALTFPKSMRW GNRRLRFIRP VRWLVGLFGE EVVPFTWAGV
     TADKVTRGHR FLGAEATIPV AEQYEDILKE QAVVVDIEAR RADIRSQLAR LEKEKGWQIP
     IDGDLLEEVT HLVEFPTALS GSFDEAYLEL PASVLITTMR EHQRYFPVED ANGKLLPFFI
     TVRNGDECSL GKVAKGNEKV LSARLADARF FFEEDQKLSI EKAVEKLNNV IFFEGLGTIG
     DHVHRIRALA ETLADRLELE DGERKTLLRA ADICKFDIST YMVNEFPELS GVMGQVYAKQ
     AGESEDVAEA IEEHYYPRFA NDRSPKGSAG TLISLLDKLD GVVAAFSLGI QPTGSQDPYS
     LRRRAAGVIQ ILADSTWKSL TLSTLFDLAL DQLTEDGWLK RPADEVKDEL TAFFDLRLKA
     LLQEEGIRYD IIDALLTGES TTPSLMLDKA RVLVREVEKD EFKQVVEGFS RAANLADKGE
     PGLTINRDLL EAWAERELLA TIGNAGEAFT KAEARQDAQG MYDEISKLAP VIHRFFDDVL
     VMDENVANRN NRLALLQQID ALVSRFALFK KIVFAS
//

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