ID   SYGB_SOLM1              Reviewed;         697 AA.
AC   C4XS54;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=DMR_20850;
OS   Solidesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1)
OS   (Desulfovibrio magneticus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Solidesulfovibrio.
OX   NCBI_TaxID=573370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700980 / DSM 13731 / RS-1;
RX   PubMed=19675025; DOI=10.1101/gr.088906.108;
RA   Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., Aoki N.,
RA   Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., Takeyama H.,
RA   Matsunaga T.;
RT   "Whole genome sequence of Desulfovibrio magneticus strain RS-1 revealed
RT   common gene clusters in magnetotactic bacteria.";
RL   Genome Res. 19:1801-1808(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; AP010904; BAH75576.1; -; Genomic_DNA.
DR   RefSeq; WP_015860762.1; NC_012796.1.
DR   AlphaFoldDB; C4XS54; -.
DR   SMR; C4XS54; -.
DR   STRING; 573370.DMR_20850; -.
DR   EnsemblBacteria; BAH75576; BAH75576; DMR_20850.
DR   KEGG; dma:DMR_20850; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_7; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000009071; 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.
FT   CHAIN           1..697
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_1000204602"
SQ   SEQUENCE   697 AA;  75148 MW;  25F7CCE2127A2494 CRC64;
     MSHFLFEIGF EEMPARFLPG LVDEVKKLFA EGLTQAKVDC GTIAAFATPR RLVVSVPDLA
     AAARREEEVV SGPPEKVGFD AAGAPTKAAE GFAKGQGLDV SAVFVMDTPK GRYLALRKTT
     GGEAAIELLP ALCLEAVKKL SFPKRMRWGS REFAFGRPVH WFLALLDDAV VPFQFDDITS
     GRATYGQRIM GPGPFEVPTA AAYFDIIRDK GKVVLDARER EGIVRSQAEA LAKEAGGTAV
     INPALLAEVT GLTEHPVVLL GRFDPKFLDV PREVLITSME SHQKSFAVED GKGGLLPVFL
     TTLGLVPGNV ELVRRGWQRV LTARLEDARF FWEADLSASL ETWQKKLENV VFLAGLGSMR
     DKGKRLERLC GLIAEQAGKP EIMLEASQAG GLAKVDLVSD MVGEFAELQG IMGGIYSRRK
     GQSKTASRAV AEQYLPAGPD SPVPATLAGA ILSIADKADT LAGCFGLDMA PTGAADPYAL
     RRAALGICRV VIEHGLRLDL MELLQGAIDG YGEVKFKVDR THVLAKLLDF FGQRLKAYFT
     GQGYDTLVVE AALGASYTDI AALSARLSAL AGFAAKPDFD QAVLTFKRAA NIIRKQGVGA
     GVPLTGAVKA ALLEEQAEKD LAAVCQDVFP RFDALFDAGD YGAVLELLYE LRPSVDAFFD
     NVMVMCDDMD MRLNRLNLLK SLVDRLGRVA DFAALQV