SYGB_ANASK
ID SYGB_ANASK Reviewed; 701 AA.
AC B4UG87;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=AnaeK_2554;
OS Anaeromyxobacter sp. (strain K).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC unclassified Anaeromyxobacter.
OX NCBI_TaxID=447217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K;
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., Ovchinnikiva G.,
RA Beliaev A.;
RT "Complete sequence of Anaeromyxobacter sp. K.";
RL Submitted (AUG-2008) 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; CP001131; ACG73779.1; -; Genomic_DNA.
DR RefSeq; WP_012526563.1; NC_011145.1.
DR AlphaFoldDB; B4UG87; -.
DR SMR; B4UG87; -.
DR EnsemblBacteria; ACG73779; ACG73779; AnaeK_2554.
DR KEGG; ank:AnaeK_2554; -.
DR HOGENOM; CLU_007220_2_2_7; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000001871; 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 SMART; SM00836; DALR_1; 1.
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..701
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000197168"
SQ SEQUENCE 701 AA; 75745 MW; 391A2CA4F2EA58BF CRC64;
MADLLFEIGA EEIPAGFVPG ALRQLEDDLA KALADARLAH GEVRSVGTPR RLAVWARDVA
PKQTDARTEA FGPPVAQAYD AEGKPTPAAT GFARSQGVEV SALVRAQTPK GERVAVTKVE
KGRRAEQVLP ALLERLVGGL RFRKAMRSRF DEATFARPVR WMVALLGGRP LKVRHGEVTS
GKVTYGHRFL APKAIALKGT PDDYLAKLRR AHVLADPVER RAALLAELAR AGKEAAGKVR
EDPALVEQVL YLVEEPTAVV GEFEKSNLEL PPEVVISEMR NHQRYFAVVD GKGRLKNRFV
AVSATRVKDP AVARHGYERV LRARLADARF FFEEDRKRKL HERIEDLGRR TFQAKLGSEL
DRAQRIGAVA SALARALGKD ALVADLLEAS RLAKVDLNTG MVGEFPELQG TMGAHYARLE
GLKPEIADAI EDHYKPIGAA EELPRSDLGA LVAVADRLHS LVGIIGVGEK ATGAADPFGL
RRAAIGILRI VIARGYHLSL AAAVEQTLDA LSGVKLAAGR ALVAEQVLDF LRGRVRAAWT
ERFDADLVEA VLAAGSDDVV DARRRLEALA DAKARPDFGS LAVAFKRVAN IQEKAGGSGA
AAVDPALLRD AAEKDLLAAL EKVEQEVVAR RAARDYPAVL RTVATLEPAV ARFFDGVLVM
AEDPALRANR LGLMRRVAAL FSDLADFRKI QAEAPAQARA G