SYGB_DESAL
ID SYGB_DESAL Reviewed; 690 AA.
AC B8FKD8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=Dalk_0043;
OS Desulfatibacillum aliphaticivorans.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfatibacillum.
OX NCBI_TaxID=218208;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK-01;
RX PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT for anaerobic alkane oxidation.";
RL Environ. Microbiol. 14:101-113(2012).
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; CP001322; ACL01753.1; -; Genomic_DNA.
DR RefSeq; WP_012609193.1; NC_011768.1.
DR AlphaFoldDB; B8FKD8; -.
DR SMR; B8FKD8; -.
DR EnsemblBacteria; ACL01753; ACL01753; Dalk_0043.
DR KEGG; dal:Dalk_0043; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_2_7; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000000739; 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..690
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000204600"
SQ SEQUENCE 690 AA; 75448 MW; CA402966AC7FF184 CRC64;
MQPLLLEIGS EEIPAGYIVP ALEALAQALD AKLESARIAH SKPKVYGTPR RLAVILDEVA
EKQESVTTEM VGPPKSVAFD GEGKPKVPAV KFAEKAGVAV EELTFQETEK GVYLCAKIQD
EGKETLGILQ EMLPEIISHI PFPKSMRWAA LPGTFARPVF SILALLGDQV IPFEWNGVTT
GRQTRGHYFM APEAIDIQTP SEYVNALEKA KVIADIPTRR KMVKEGVDAI AKELGGDAIE
DEELVDIVAN LVEFPAPVGG KFETGFLEVP DKVLITAMRE HQKYFAIQDK DGKLMPCFVA
VNNTQCKDPQ LVATGHERVL RARLSDAKFF WDVDKKQSME DWVKRLDRVL FQKKLGSVGE
KVARVEEMAK FLAAAPEING DPDKAQKAAH FCKADLVSGL VIEFTKLQGV MGKAYASLAG
MDAETASALE EHYLPAYSGG PLPRTKTGDA VAMADKMDSL CGCFAVGLIP SGNRDPYALR
RQGIGVIRIL QEKGYSLSLS AIVDKGLTLV KDKADQNLAE TRDKIISFLA DRMAHMLAEQ
GFSKDVIQAA VAISCDDIPY LWKRVAAVEK LKTLPDYEAL AQTFKRVANI IKQAAEKGTL
SDQEVNPALF EKDCEKDLLE AFTAMEAKVS GLGVDEALLE VAKLRPAVDA FFDDVMVMAE
DMKVRENRLA LLAGIAGLFG RFADFSRISA