SYGB_RICAH
ID SYGB_RICAH Reviewed; 662 AA.
AC A8GQ64;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-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=A1C_06580;
OS Rickettsia akari (strain Hartford).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=293614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hartford;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia akari.";
RL Submitted (SEP-2007) 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; CP000847; ABV75539.1; -; Genomic_DNA.
DR RefSeq; WP_012150168.1; NC_009881.1.
DR AlphaFoldDB; A8GQ64; -.
DR SMR; A8GQ64; -.
DR STRING; 293614.A1C_06580; -.
DR EnsemblBacteria; ABV75539; ABV75539; A1C_06580.
DR KEGG; rak:A1C_06580; -.
DR eggNOG; COG0751; Bacteria.
DR HOGENOM; CLU_007220_2_1_5; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000006830; 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..662
FT /note="Glycine--tRNA ligase beta subunit"
FT /id="PRO_1000101327"
SQ SEQUENCE 662 AA; 75145 MW; D66ADB0E50F98E34 CRC64;
MSELLLELFS EEIPAFMQKN AEEGYLNIFT QIFAESAIFA KVQVFVGPRR ITLYATHLPK
VTLPQEEEIK GPSIESPEAA INGFCSAHNV SKLELSTKLI NNQLYYFFVK KTKEREIKEI
LPKIIIEAIN KYSWAKSMFW GDYKIKWIRP LRNILCIFDG EVLPLQFGHL TANNITYGHR
LTDNKKLEVT DFKDYRNKLL ENNVVLERIK REEIIKTGLL ELANSQNLNI KEDARLIEEV
AGLSEFPVVL LGKIAQKFLE LPKEVLIASM RTHQKYFCLF DKTGNFAPYF LFVSNGRFAN
AELVIQGNEK VLSARLSDAL YFYKQDIAKT LESRLGKLEA VTFHAKLGNL REKIEHITDI
CNYIAPNNKD LITAAKLCKS DLVSEMVGEF PDLQGIMGYY YAKYEGLNEE IAAAIRDHYK
PQGLSDNVAS GNAALLALAD KLDSLVGLMI AGEAPTGSGD PYALRRQALG IIRIILENKL
ELNLNDLIIF SLKLYGNSAD KDLITSFFEE RAKFYFKNKY DILLINAVLD LNLVDTQFKL
ETLKEFLIED AGKQLLNAYK RASNIIGDQK ITGLVDASLF STQPEKDLFE VVQKISPQII
DSIADKDYKR ALNLLSFLLT PITSFFDNVL VNDPDPKIAQ NRLSLLQNIC ELLNKIAKFN
RL