UniProt: S6BPR3

Database: UniProt
Entry: S6BPR3_9GAMM

LinkDB:  S6BPR3_9GAMM 
Original site:  S6BPR3_9GAMM

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (3)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (17)   

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ID   S6BPR3_9GAMM            Unreviewed;       695 AA.
AC   S6BPR3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
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:BAN68004.1};
GN   ORFNames=EBS_0008 {ECO:0000313|EMBL:BAN68004.1};
OS   endosymbiont of unidentified scaly snail isolate Monju.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1248727 {ECO:0000313|EMBL:BAN68004.1, ECO:0000313|Proteomes:UP000015562};
RN   [1] {ECO:0000313|EMBL:BAN68004.1, ECO:0000313|Proteomes:UP000015562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Monju {ECO:0000313|EMBL:BAN68004.1};
RX   PubMed=23924784; DOI=10.1038/ismej.2013.131;
RA   Nakagawa S., Shimamura S., Takaki Y., Suzuki Y., Murakami S., Watanabe T.,
RA   Fujiyoshi S., Mino S., Sawabe T., Maeda T., Makita H., Nemoto S.,
RA   Nishimura S., Watanabe H., Watsuji T., Takai K.;
RT   "Allying with armored snails: the complete genome of gammaproteobacterial
RT   endosymbiont.";
RL   ISME J. 8:40-51(2014).
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; AP012978; BAN68004.1; -; Genomic_DNA.
DR   RefSeq; WP_043106729.1; NZ_AP012978.1.
DR   AlphaFoldDB; S6BPR3; -.
DR   STRING; 1248727.EBS_0008; -.
DR   KEGG; enm:EBS_0008; -.
DR   HOGENOM; CLU_007220_2_2_6; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000015562; Chromosome.
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:UP000015562}.
FT   DOMAIN          582..678
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   695 AA;  77957 MW;  4BCD077AD71F86C5 CRC64;
     MSDRADLLFE LGTEELPPTA LKRLSSALEE GFLTGLSEAQ LAHGEVIAYA TPRRLALLVR
     DLEQRQPDRD VERRGPAVKA AFDAEGRPTK AAEGFARSCG TTVDQLERLE TDKGEWLVFR
     SHQPGQPAAE LLPAIAERAL ERLPIPKRMR WGDSEAQFVR PVHWLVFLHG DAVVECTLLD
     TPAGRVTRGH RFHHPEGITL YDPADYAAIL ENVGKVIAYF PDRRSRIRAQ VEATAKKLGG
     VADIDEALLD EVTALNEWPV PVAGSFDADF LEVPHEALVS TMKGNQKYFP VFDAEGRLLN
     HFITIANIES REPEMVRAGN ERVIRPRLAD ARFFWEQDGK KRLEDHIDSL RDVVFEKRLG
     SMYEKSERVA ALAARIAEQI GGDVEKARRA GMLSRCDLMT EMVYEFPDMQ GIMGRYQALR
     DGEDPELAHA LDEFYMPRFS GDRLPETRTG IAVALAERLD TLVGIFGIGM KPTGDKDPYA
     LRRAALGALR ILREHSLSLN VLELLDQARE QLGDRLDDNG VVETVWQFMR DRLRRLYADA
     GVSADIFEAV ITVAPPDLAD IEQRIRAVQA FLKLPEAEAL IAANKRIGNI LKKAGENIPR
     TVDPERFEET AEQVLLDEIK TVEGGLLLRT DDYIKQLETL ARLREPTDRF FDEVMVMAED
     PLVRNNRLAL LRRARELFLQ VADIGRLQAG GGESA
//

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