SYGB_AQUAE
ID SYGB_AQUAE Reviewed; 664 AA.
AC O67898;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Glycine--tRNA ligase beta subunit;
DE EC=6.1.1.14;
DE AltName: Full=Glycyl-tRNA synthetase beta subunit;
DE Short=GlyRS;
GN Name=glyS; OrderedLocusNames=aq_2141;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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;
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AE000657; AAC07870.1; -; Genomic_DNA.
DR PIR; F70483; F70483.
DR RefSeq; NP_214467.1; NC_000918.1.
DR RefSeq; WP_010881403.1; NC_000918.1.
DR AlphaFoldDB; O67898; -.
DR SMR; O67898; -.
DR STRING; 224324.aq_2141; -.
DR PRIDE; O67898; -.
DR EnsemblBacteria; AAC07870; AAC07870; aq_2141.
DR KEGG; aae:aq_2141; -.
DR PATRIC; fig|224324.8.peg.1655; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_0; -.
DR InParanoid; O67898; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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..664
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_0000072892"
SQ SEQUENCE 664 AA; 77524 MW; 7FFEF7A8F552E3DB CRC64;
MTNELLIEIG TEELPAGVIN PALDYLKDKI NSLLNARQVK TYGTPRRLTL YFKDFENERK
EKKEVIWGPP KNVAYDEKGN PTKALEGFLK KNNASLEEVK VLKKDKGEYV AIVRKVIEKS
PIEKLQEEFE EILLSVPFPK RMRWTSSKRI TFSRPVRWIL ALFNGQVLKL RFGELESSNK
TYGHRFLSKG EVTINNPADY EKTLKEHYVI PDFNERKEII LRALEKSSQE VGGKPSYPEG
LVEEVTNLVE YPFPVLGKFD EKYLELPPLV ITTVAAHHQR FFCFEKDGKL LNYFLGISNN
KPNEKIKEGY EKVLRARLED ALFFYREDLK KDLKSLIPEL KKVLFHPKVG SMYEKEERME
KIAQKLCPLL KCEWEKVKEA VWLSKVDLLT EMVKELDELQ GYMGYVYAKA QGYDEEVAKA
LWEQYFPRSL EDKVPETTTG TILSLSDKID NLYSFFKAGE IPKGSSDPYG LRRSAFGIIK
IVDVKNLDLN LEDFKEIYGE FKQYPKLVEF LKQRLISYLE DYPVDIVRAV LNVYSPMEPY
KVINSVRVLY EASKSPEFPS VVEAAKRVIR IIPKDWKNYE VDEKLLSEEA ERELYQKLTE
FENKELKSPL ELLPLKEYID KFFDNVKVMA EDEKIRNNRI SLLKRVENLF RTFGDFNEIV
IKEG