SYGB_MAGMM
ID SYGB_MAGMM Reviewed; 700 AA.
AC A0L7K9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=Mmc1_1441;
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX PubMed=19465526; DOI=10.1128/aem.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(2009).
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; CP000471; ABK43952.1; -; Genomic_DNA.
DR RefSeq; WP_011713105.1; NC_008576.1.
DR AlphaFoldDB; A0L7K9; -.
DR SMR; A0L7K9; -.
DR STRING; 156889.Mmc1_1441; -.
DR PRIDE; A0L7K9; -.
DR EnsemblBacteria; ABK43952; ABK43952; Mmc1_1441.
DR KEGG; mgm:Mmc1_1441; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_5; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000002586; 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..700
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000197206"
SQ SEQUENCE 700 AA; 76198 MW; 9EB2AF82847588A2 CRC64;
MAEFMWEIGT EEIPARMLPG AITAMGELTR TALQEAGLGF AQVESQGTPR RLLVVVHGLH
DKQADVQEER RGPALQAAFD SDGNPTKAAQ GFARGCGVDV DQLSRVETPK GTYLSYTLKQ
AGKGASEVLP GIMQQVFKAL PWPKTMRWSD GESRFVRPVQ SVTALLNGQQ VAVELAENVR
YTDAVSGHRF MGKGAVVVQD YASYQQAMAD GKVMLKSEDR MATIRAGVLA QAASVGGVVA
SDEGLVAENA SLTEWPVALL GRFDERYLEI PPEVLTTSMR YHQKYFPVLD AQGGLKPHFV
VIANMETEDQ TVLVRGYQRV LKARLEDAAF FWAEDRKIRL TDRLPDLQAV VWQAKLGSLF
QKSQRMAHLA SAIAARVAPQ QAALAEKAGL YSKCDLVTGM VGEFPELQGI MGGYYLPRER
AQDEVVALAI REHYMPAGAG DALPQSLCGR IVSLADKLDT LVGCFGMGIT PTGTKDPFGL
RRAALGVIRL LLQEQGLRLP LRQLCEEAYR QYGEIGLEMG EAQTVQGVLA FFYGRLQAHL
KAEGVDYDLI DAVQGLNLDD LWDAVSRVKA LVAFKQDAAY EALVAANKRM ANILSKVEDS
ALDLTLGVDE AVLKASAEQG LAAAVAAVED RVKTHSSNGR YAEALGELAA LRGVIDTFFD
EVMVMDEDDA VRHNRLRLLA TVLGLFRQVA DVSCLVVAEK