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Database: UniProt
Entry: F4QRA8_9CAUL
LinkDB: F4QRA8_9CAUL
Original site: F4QRA8_9CAUL 
ID   F4QRA8_9CAUL            Unreviewed;       682 AA.
AC   F4QRA8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE            EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00255};
DE   AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE            Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00255};
GN   Name=glyS {ECO:0000256|HAMAP-Rule:MF_00255};
GN   ORFNames=ABI_37780 {ECO:0000313|EMBL:EGF90745.1};
OS   Asticcacaulis biprosthecium C19.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF90745.1, ECO:0000313|Proteomes:UP000006512};
RN   [1] {ECO:0000313|Proteomes:UP000006512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C19 {ECO:0000313|Proteomes:UP000006512};
RA   Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Draft genome sequence of Brevundimonas diminuta.";
RL   Submitted (MAR-2011) 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:0000256|ARBA:ARBA00000201,
CC         ECO:0000256|HAMAP-Rule:MF_00255};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00255}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00255}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00255}.
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DR   EMBL; GL883079; EGF90745.1; -; Genomic_DNA.
DR   RefSeq; WP_006274559.1; NZ_GL883079.1.
DR   AlphaFoldDB; F4QRA8; -.
DR   STRING; 715226.ABI_37780; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_5; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000006512; Unassembled WGS sequence.
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   NCBIfam; TIGR00211; glyS; 1.
DR   PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00255};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00255}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00255};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00255};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00255}.
FT   DOMAIN          574..668
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   682 AA;  74365 MW;  3D08B76C5F068DDB CRC64;
     MPQLLIELFS EEIPARMQLG AARDFERLFG AKLNTSGLSF ESIKAYVAPR RLALVVEGLP
     AEQAAVTEEV KGPKDGAPEQ AMAGFLRKVG LTQDQLVLEN GVWMARIEKP GRRTVDALPD
     MLREVILAFP WPKSMRSGVS SFRWVRPLKR ILFLFDGQIV PFELEGLTAS SLTEGHRFLG
     SGKALNVSDF ASYHKALADN SVILDHAERQ AFILKEAKAV CEDTGCELIE DQGLLEEVAG
     LNEFPMPILG DMDPKFLALP PEVIKTSMRT HQKYFAVRDK ATGKMAPHFI IVANIRARDG
     GDEIKRGNAK VLSARLSDGV FFWNEDNKAG NFDGWLERLK GTTFHVKLGT MAQRVERISA
     LAAHIAGHLG ADIAAAREAA RLAKADLASK MVGEFPELQG VMGGYYADAL KLKPEIADAI
     REHYKPQGPS DSVPAGKVSA AVALADKIDT LVGFFAIGEK PTGSKDPYAL RRSALGVLRI
     IREHGATLHL GGLVDAWYRS RGELPVAVQD VEAVRPEVLD FFADRLKVQL RDEGRRFDVL
     EATRGSDDVV NTITRIEAVE AVIATPQGED LLTLHKRAAN ILAASKTDLS HAMPQAYEGI
     DPLEKALLEA LNVARSDVVS HISEENYAGA LKSIAALRQN VDSFLDGVLV NADDEKVKVN
     RLAILRGVCE LSAPIADLSK IA
//
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