SYGB_OCEIH
ID SYGB_OCEIH Reviewed; 692 AA.
AC Q8EPY2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 123.
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=OB1948;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC13904.1; -; Genomic_DNA.
DR RefSeq; WP_011066345.1; NC_004193.1.
DR AlphaFoldDB; Q8EPY2; -.
DR SMR; Q8EPY2; -.
DR STRING; 221109.22777632; -.
DR PRIDE; Q8EPY2; -.
DR EnsemblBacteria; BAC13904; BAC13904; BAC13904.
DR KEGG; oih:OB1948; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_9; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR PhylomeDB; Q8EPY2; -.
DR Proteomes; UP000000822; 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..692
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000006380"
SQ SEQUENCE 692 AA; 79558 MW; 52DAAB4B2E5877F6 CRC64;
MARDVLIEIG LEELPARFID DAELQLYTKT KQWLEENRIS SENVISYSTP RRLAVFVKNM
AEKQSSIEED VKGPALKIAK DEDGNWTKAA QGFTKGQGLT TDDIVVREVK GISYIYVTKH
IEGRPIQELL PEFKSIIESI TFGKNMRWGS ETIRYARPIR WLVAMMGNEV IPFEIAHVAT
NNVTYGHRFL GEEVTIQEPA EYEKTLKDNY VIVKAKDRET LIVEQLSKLE REHGFEIPVD
QELLEEVRNL VEFPTAFVGK FEEAYLEIPP EVLITSMKEH QRYFPVHKKG VLQPYFVGVR
NGDNYHIETV AKGNEKVLRA RLADAEFFYN EDLHQSIDFF QEKLTKVVFQ EKLGTYSDKV
ERMKQIADRI SEKLSLESDD RKIIERAAEI SKFDLMTSMV NEFTELQGII GEKYANHFGE
NSATSQAIKE HYQPKHAKDD LPQTVIGSVV SVADKLDTIA GCIAVGLVPT GSQDPYGLRR
QASAILRILH NEKWNLTVEE LIDIALDVFQ KSNVTIMEKT NEELIEFFRL RAVYLMKDKG
LEVDVIHAVT DQKLGNVFVS FEKAKELSDK RNDETFKPIQ EALVRVLNLS NKVETNELIR
EDKLETESEK ILYTRYLDIK ETYEKQLLHN ETKQALATLA QLAAPIHAFF DNNMVMADDL
EIRNNRLALI QALTSLILPY ADLRKIEWKQ QF