SYGB_HAHCH
ID SYGB_HAHCH Reviewed; 692 AA.
AC Q2SQY0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-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=HCH_00021;
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396;
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
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; CP000155; ABC26944.1; -; Genomic_DNA.
DR RefSeq; WP_011394021.1; NC_007645.1.
DR AlphaFoldDB; Q2SQY0; -.
DR SMR; Q2SQY0; -.
DR STRING; 349521.HCH_00021; -.
DR PRIDE; Q2SQY0; -.
DR EnsemblBacteria; ABC26944; ABC26944; HCH_00021.
DR KEGG; hch:HCH_00021; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_6; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000000238; 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 SMART; SM00836; DALR_1; 1.
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..692
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006367"
SQ SEQUENCE 692 AA; 77189 MW; BD1F2472A7E1D73C CRC64;
MNHQDFLVEI GAEELPPKAL RQLAEAFAQG IRQRLEKAQL SFSELTWYAA PRRLAVHVSG
LAEKQPDLEV EKRGPALQAA FDAAGAPTKA CEGFARSCGT TPDKLEKLET DKGVWLVFRS
KQAGAPTTGL LPAIVEESLA ALPIPKRMRW GARRTEFVRP VHWIIMLFGE KVIDCEILGL
KAGNTTLGHR FHHPAPIEIA TPANYKDALK NTGYVMADFE ERKALIRQQV EAIAKQTSGM
AVIDEELLEE VASLNEWPTA LMGRFEDRFL EVPAEALIST MKGNQKYFHV VDAEGRMLPY
FITVANIESK DPQQVIDGNE RVIRPRLSDA AFFFSTDKKR TLASRLEDLK PIVFQQQLGT
VYDKAIRVGK LAAKIAAKID SNPEWAQRAG ELSKTDLATE MVMEFPELQG TMGRYYAAID
SEPEEVSMAQ EEQYLPRFAG DQLPTTLTGC AVSLADKLDT IVGIFGINQP PTGAKDPFGL
RRAALGVLRI LVEKKLDLDL AECVQWAQEL HGDLPAENLE TAVVDYMLDR FRAWYEEAGV
PTEVFLSVLA RRPTKPVEFD QRVLAVAEFL KLDAAQALAA ANKRVSNILS KEQVDISAES
ANPELFTEEA EKNLFRALQE KSESARPYIE QRNFTQALQQ LAELKDVIDL FFDKVMVMVD
DPAIRSNRMT LLASLRHVFL QVADISLLQN KA