UniProt: A0A1I2XG20

Database: UniProt
Entry: A0A1I2XG20_9FIRM

LinkDB:  A0A1I2XG20_9FIRM 
Original site:  A0A1I2XG20_9FIRM

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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   A0A1I2XG20_9FIRM        Unreviewed;       695 AA.
AC   A0A1I2XG20;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-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   ORFNames=SAMN05660649_03955 {ECO:0000313|EMBL:SFH12362.1};
OS   Desulfotruncus arcticus DSM 17038.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC   Desulfotruncus.
OX   NCBI_TaxID=1121424 {ECO:0000313|EMBL:SFH12362.1, ECO:0000313|Proteomes:UP000199337};
RN   [1] {ECO:0000313|Proteomes:UP000199337}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17038 {ECO:0000313|Proteomes:UP000199337};
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|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; FOOX01000017; SFH12362.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2XG20; -.
DR   STRING; 341036.SAMN05660649_03955; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000199337; 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:UP000199337}.
FT   DOMAIN          585..681
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   695 AA;  77985 MW;  8DED33A7EA70B0C6 CRC64;
     MARDFILEIG MEELPARFIA PSVEQMRQLA GKALRDSRIA YKEIKTYGTP RRIAILISDL
     AEDQEALIQE AKGPAVKVAF NAAGEPTRAA QGFAKSQGVQ VEDLVRKSVG PVEYVFALKK
     EEGGKTFAVL PAIALALIEG LHFPKPMRWG DLEVRFARPI RWLLCLYGKD VVKFEFAGLR
     SDRYTMGHRF LSYGKVEITD AGSYCRVLEE AFVMADIDQR KSKIRSQIEQ AAVEKGGRPE
     TNEELLDEVT NLVEYPTALC GSFDGRYLEM PEEVLITPMR EHQRYFPVRG SDDRLLPLFV
     AVSNGGAGNV DIVRAGNEKV LRARLSDAAF FWQEDLKAPL EDKVDRLKKV IFQESLGTIY
     EKVQRITNLA DYIGGRLGAP PEERSNLLRA ARLAKADLLT NMVYEFPELQ GIMGREYARR
     FNEPEGVALA IYEHYLPRFA GDDLPDTLPG KILSIADKLD TLVGCFGVGI QPTGSQDPYA
     LRRQALGICH IILDAGLTLS LAEMIEQAYN NYADRVKMKL GVDQVISELG EFFKQRLRVL
     FIERGLSYDT VDAVLAPGYD AAYDTWLRGK ALEQFRSEPA FEALLTAFTR AYNLSKKTES
     DQVAPALFET EVERELYAAF HQVSKAAGDS CQAREYNTAF SLIAELQKPV DRFFEDVMVM
     VEDPRIRDNR LALLKNIADF IGRVADLSKL VVQNK
//

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