SYGB_ANAD2
ID SYGB_ANAD2 Reviewed; 701 AA.
AC B8JDD8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=A2cp1_2650;
OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=455488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-1 / ATCC BAA-258;
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 Beliaev A.S., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL Submitted (JAN-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; CP001359; ACL65987.1; -; Genomic_DNA.
DR RefSeq; WP_012633767.1; NC_011891.1.
DR AlphaFoldDB; B8JDD8; -.
DR SMR; B8JDD8; -.
DR EnsemblBacteria; ACL65987; ACL65987; A2cp1_2650.
DR KEGG; acp:A2cp1_2650; -.
DR HOGENOM; CLU_007220_2_2_7; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000007089; 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_1000197166"
SQ SEQUENCE 701 AA; 75777 MW; 464D5DAB95AAA5EA CRC64;
MADLLFEIGA EEIPAGFVPG ALRQLEDDLS KALADARLAH GEVRSVGTPR RLAVWARDVA
PKQTDARTEA FGPPVAQAYD AEGKPTPAAT GFARSQGVEV SALVRAQTPK GERVAVTKVE
KGRRAEQVLP ALLERLVGGL RFRKAMRSRF DEATFARPVR WMVALLGGRP LKVRHGEVTS
GKVTYGHRFL APKAIALKGT PDDYLAKLRR AHVLADPVER RAALLAELAR AGKEAAGKVR
DDPALVEQVL YLVEEPTAVV GEFEKSNLEL PPEVVISEMR NHQRYFAVVD GKGRLKNRFV
AVSATRVKDP AVARHGYERV LRARLADARF FFEEDRKRRL HERIEDLGRR TFQAKLGSEL
DRAQRIGAVA SALARALGKD ALVADLLEAS RLAKVDLNTG MVGEFPELQG TMGAHYARLE
GLKPEIADAI EDHYKPIGAA EELPRSDLGA LVAVADRLHS LVGIIGVGEK ATGAADPFGL
RRSAIGILRI VIARGYHLSL AAAVEQTLDA LSGVKLAAGR AVVAEQVLDF LRGRVRAAWT
ERFDADLVEA VLAAGSDDVV DARRRLEALA DAKARPDFGS LAVAFKRVAN IQEKAGGSGA
AAVDPALLRD AAEKDLLAAL EKVEQEVVAR RAARDYPAVL RTVATLEPAV ARFFDGVLVM
AEDPALRANR LGLMRRVAAL FSDLADFRKI QAEAPAQARA G