SYGB_PHEZH
ID SYGB_PHEZH Reviewed; 669 AA.
AC B4R9A9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 64.
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=PHZ_c1365;
OS Phenylobacterium zucineum (strain HLK1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=450851;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLK1;
RX PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT "Complete genome of Phenylobacterium zucineum - a novel facultative
RT intracellular bacterium isolated from human erythroleukemia cell line
RT K562.";
RL BMC Genomics 9:386-386(2008).
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; CP000747; ACG77779.1; -; Genomic_DNA.
DR RefSeq; WP_012521923.1; NC_011144.1.
DR AlphaFoldDB; B4R9A9; -.
DR SMR; B4R9A9; -.
DR STRING; 450851.PHZ_c1365; -.
DR EnsemblBacteria; ACG77779; ACG77779; PHZ_c1365.
DR KEGG; pzu:PHZ_c1365; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_1_5; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000001868; 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..669
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101314"
SQ SEQUENCE 669 AA; 73165 MW; 403DED50DAB7B0AC CRC64;
MPQLLLELLS EEIPARMQAQ AARDLERLAR ERLAAEGLLP EALKTFAGPR RLTLVAEGLP
AAQADRREEL KGPKVGAPEQ ALEGFLRKTG LTRDQLVERD GVFFATIEKP GRPTPEIVAE
MVEAILRTFP WPKSMVSGTS KLRWVRPLRR ILCVFDGEVV PFEVDGIASG DLSEGHRFMS
DGQPFLVKDF EGYAAGLSHR SVVLDADERK ERILEAAKTL CFARNLELVE DAGLLDEVAG
LVEWPVPVLG DMDPAFLDLP PEVIRTSMRV HQRYFAVRDP AGGKLAPHFL TVANIAARDG
GATIAKGNAK VLSARLSDAR FFWDEDRKVR LEDRLEKLKG VTFHAKLGTM YERVQRIEAL
AGELAPFVRD EPETRTKAVQ AARLAKADLV SGVVGEFPEL QGIMGGYYAE AEGLDPEVVD
AIRSHYRPQG PNDAVPVSSV AATVALADKL DTLVSFFGIG EKPTGSRDPF ALRRAALGVI
RIVLETRTRL PLKRFVSDEV LDFFADRLAV LLREQGKRHD LVAAVFALGD DDLVRIVARV
EVLSAFLKTE DGANLLAGYK RAVNILRAEE KKGPLPAGEP AQAAGAPAEE AALVQAVAAL
DARLGPALER EDFEGAMTEL AKLRGPVDAF FDKVLVNSDV PAERENRLRL LAKVRDAMGR
VADFSQVTG