SYGB_GEOSM
ID SYGB_GEOSM Reviewed; 687 AA.
AC C6E0B4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 61.
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=GM21_0656;
OS Geobacter sp. (strain M21).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter; unclassified Geobacter.
OX NCBI_TaxID=443144;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M21;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Lovley D.;
RT "Complete sequence of Geobacter sp. M21.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001661; ACT16730.1; -; Genomic_DNA.
DR RefSeq; WP_012774350.1; NC_012918.1.
DR AlphaFoldDB; C6E0B4; -.
DR SMR; C6E0B4; -.
DR STRING; 443144.GM21_0656; -.
DR EnsemblBacteria; ACT16730; ACT16730; GM21_0656.
DR KEGG; gem:GM21_0656; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_7; -.
DR OMA; LPIPKRM; -.
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.
FT CHAIN 1..687
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000204605"
SQ SEQUENCE 687 AA; 75808 MW; ACBF54EF43EDA723 CRC64;
MAKDLFLEIG CEEIPAGFVP KAMADMELLI KKEFDSARIE YGEIVTLGTP RRLVLAVKGV
AERQPDAELT AMGPAKSHAY DADGNPTKAA QGFARGQGID VSQLKLVTTE KGEYLAAVKS
EIGRETAELL PEMLPRLIGN IPFKKSMRWA DFDVRFARPI HWIAALFDGK VVPFSFGNID
SGSASRGHRF MANTPFPVRD LAHYLEECER HFVIPDPNKR KEIIRAEIER VAKQAKGNVL
PDEALLEQVS YLVEYPSAVH GTFSPDFLVV PREVLITSMR EHQRYFSLVD DEGKLLPGFI
TINNTITEDP QVVVKGNERV LRARLSDARF FFDEDHKVRL ETRVESLKSV VYQAKLGTSY
EKMERFRELG KRLAQRLNPS VIKQVERAAT LCKADLVSGM VGEFPEVQGI MGREYALHDG
EEPAVANAIA EHYLPTQAGG ELPASDIGAF VSLADKMDTI CGCFCVGLIP TGSADPYALR
RSALGIINII LEKGYREPLS EFVKASLDLL AAKATRPLAE VQKDVLDFFR GRFVNLMADR
FPSDAVEAVA SVSFDDLVEA AAKIEALAGF RNRDDFGPLA VAFKRVCNIV KDGVDTPVSA
ELFQDAAEGE LHQALTQVSG KVADALKKAD YLAALTEIAT LKPAVDLFFE KVMVMADDER
VRQNRLALLT GIARLFASLA DFSRLSP