SYGB_SYNAS
ID SYGB_SYNAS Reviewed; 690 AA.
AC Q2LVI9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00255};
DE AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000255|HAMAP-Rule:MF_00255};
DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00255};
GN Name=glyS {ECO:0000255|HAMAP-Rule:MF_00255}; OrderedLocusNames=SYNAS_22160;
GN ORFNames=SYN_01537;
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB;
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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:0000255|HAMAP-Rule:MF_00255};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00255}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00255}.
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DR EMBL; CP000252; ABC78095.1; -; Genomic_DNA.
DR RefSeq; WP_011418115.1; NC_007759.1.
DR AlphaFoldDB; Q2LVI9; -.
DR SMR; Q2LVI9; -.
DR STRING; 56780.SYN_01537; -.
DR PRIDE; Q2LVI9; -.
DR EnsemblBacteria; ABC78095; ABC78095; SYN_01537.
DR KEGG; sat:SYN_01537; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_7; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000001933; 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 PANTHER; PTHR30075; PTHR30075; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01045; TRNASYNTHGB.
DR TIGRFAMs; TIGR00211; glyS; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..690
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006417"
SQ SEQUENCE 690 AA; 77603 MW; C33A34B4D1DBD80F CRC64;
MSNELLLEIG TEEIPAAFLP KALQDMSSMI RKALTEARIP FGQVHTFGTP RRLCLAVADV
AEKQEDQVIE KLGPARRVSF DADGNPTKAA LGFAKSQGVD ISEIGTMQTD KGEYICISRH
ISGKSTVSLL SEMLSRLITS LSFKKSMRWG NLDFRFARPI HWILALYGGE VIPFRIENIE
SGATSRGHRF MHPEAFPVSN LQEYLARTRE HFVIVAPEER KRIILEEARK AAAAVSGRVL
ENEDLLETVT YLVEYPTIVC GSFDRKYLEL PKEVLITSMM SHQKYFPVVD QEGRLLPFFI
TINNTLARDP AVVTRGNEKV IRARLSDAQF FFEEDQKIRL DDRVEGLQQV VFHTLLGTSY
EKVQRFRKLA GWIADRIDPS LKNRVNRSAL LAKADLDTQM VGEFSELQGI MGREYALLAG
EDPTVARAIY EHYLPLTAGG DLPQTHEGAI VSIADKMDSI AGFFGVNLVP TGTADPYALR
RQALGVINII LDKKYPLTLD DLVDECISIL EEKLKRPAEE TRKDVIEFFR GRLENMLISQ
GHPHDVVSAV LAAGFADLVQ VIKKIEAMES FKAHPAYEPL AIAFKRAGNI LKEFRNGRID
PALFSAAEEN QLYSTLLEAR ARVVKALEKD DYPAALLELA ALRQPIDHFF ESVMVMVDEE
NIRFNRLSLL EALFSIFRRI ADFSRIVTES