UniProt: A0A1I4R3W5

Database: UniProt
Entry: A0A1I4R3W5_ECTMO

LinkDB:  A0A1I4R3W5_ECTMO 
Original site:  A0A1I4R3W5_ECTMO

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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   A0A1I4R3W5_ECTMO        Unreviewed;       690 AA.
AC   A0A1I4R3W5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=SAMN05421721_106109 {ECO:0000313|EMBL:SFM46630.1};
OS   Ectothiorhodospira mobilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Ectothiorhodospira.
OX   NCBI_TaxID=195064 {ECO:0000313|EMBL:SFM46630.1, ECO:0000313|Proteomes:UP000199556};
RN   [1] {ECO:0000313|EMBL:SFM46630.1, ECO:0000313|Proteomes:UP000199556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4180 {ECO:0000313|EMBL:SFM46630.1,
RC   ECO:0000313|Proteomes:UP000199556};
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|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; FOUO01000006; SFM46630.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4R3W5; -.
DR   STRING; 195064.SAMN05421721_106109; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000199556; 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:UP000199556}.
FT   DOMAIN          583..689
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
SQ   SEQUENCE   690 AA;  75835 MW;  74ECDCB65AB72980 CRC64;
     MSERSDLLIE IGTEELPPKA LTTLRDAFVD GVRRGLEAAG LAPAGARGLA APRRLAVLLQ
     GVPLRQADRP MERRGPAVQA AFDAEGRPTR AAEGFARSCG VAVADLERME TDKGAWLVYR
     HVEPGRAAQD LIPDVVAGAL AGLPIPKRMR WGDGDAEFVR PVHWVVLLLG DRVIPATILG
     VQAGGETRGH RFHHPEPLPL AAPADYLPVL EQRGHVLADF EARREVIRTQ VERAAAEAGG
     RAVVEPELLD EVTALVEWPV AVLGHFDARF LEVPQEALIS TMQDNQKYFP VVDDAGRLMP
     HFITISNVDS RELERVREGN ERVIRPRFAD AEFFWNQDRK RPLESHLEGL RQVVFQQKLG
     TLYDKTQRVT ALAEHLAGAL GAPADPVRRA ARLSKCDLQT LMVYEFTELQ GVMGRYYALH
     DGEPEAVARA LEEQYLPRQA GDALPSDTVG QVLALADRLD TLTGIFAIGL KPSGTKDPFG
     LRRAALGVLR ILVEAGLPLD LEDLLQRAAA QHDPVVSAPA AVPQVLEYML ERLRAYYQDR
     GIRPEVFEAV RAVHPTRPLD FDRRVRAVEH FRTLPQAEAL AAAHKRIHNI LRKVEGELPA
     VVDPALLAEP AEQALHARLE ALQGEVTAQL DGGDYSGGLT ALAALREPVD AFFDQVMVMA
     EDPALRDNRI ALLNQLAALF LRVADLSRLP
//

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