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Database: UniProt
Entry: A0A3M6Q192_9BURK
LinkDB: A0A3M6Q192_9BURK
Original site: A0A3M6Q192_9BURK 
ID   A0A3M6Q192_9BURK        Unreviewed;       710 AA.
AC   A0A3M6Q192;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
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=EBQ25_10435 {ECO:0000313|EMBL:RMW97027.1};
OS   Allofranklinella schreckenbergeri.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Allofranklinella.
OX   NCBI_TaxID=1076744 {ECO:0000313|EMBL:RMW97027.1, ECO:0000313|Proteomes:UP000267035};
RN   [1] {ECO:0000313|EMBL:RMW97027.1, ECO:0000313|Proteomes:UP000267035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML161473 {ECO:0000313|EMBL:RMW97027.1,
RC   ECO:0000313|Proteomes:UP000267035};
RA   Bernier A.-M., Bernard K.;
RT   "Comamonadaceae CDC group NO-1 genome sequencing and assembly.";
RL   Submitted (OCT-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RMW97027.1}.
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DR   EMBL; RDQL01000016; RMW97027.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M6Q192; -.
DR   Proteomes; UP000267035; 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}; Reference proteome {ECO:0000313|Proteomes:UP000267035}.
FT   DOMAIN          601..696
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   710 AA;  76162 MW;  89F15C8B3D6A6F77 CRC64;
     MTVNQNLLVE LFVEELPPKA LRKLGDAFAQ GIASSLQQQG LLADASAGVT AYATPRRLAV
     HLQDVAAKAA DKPVTQKLMP VSVGLQEGAP TPALLKKLAS LGLDAQAASQ LRRQGEGKNE
     ALYLDSVQPG ATLAQGLQKA LDDTIRHLPI PKVMAYQLET GVDLPGWDSV HFVRPAHGLA
     ALHGSEVVPV AALGLQSGHS TRGHRFEAQA DPIELRSADS YAEQLRDEGA VIASYAQRRQ
     AIAEQLQAAA ARIGQGSQPV QDEALLDEVT ALVERPNVLV CQFEKEFLQV PQECLILTMK
     ANQKYFPLLD AAGRLTNQFL VVSNISPEDA SAVIDGNERV VRPRLADAKF FFDTDRKKTL
     ESRVEGLNKV VYHNQLGSQG ERMQRVRAIA KALGEQLGGP ALAAAANQAA MLAKADLLTD
     MVGEFPELQG IMGGYYARHD GLSEDIAQAI EDHYKPRFAG DELPRGEVGA VVALADKLET
     LVGMFGIGNL PTGDKDPFAL RRHALGVIRI LVEKRLPLDL PATVASAAQA FGPLLPDAAK
     SNEQLLAFIY ERIAGYLREL GASAQEADAV IAARPMWGEI PKALAAVRAF AQLPEAPALA
     AANKRIGNIL KKAQDEADAQ VDQALLQEGA EQALYAAMQQ VLPQAEAQFD AGDYTASLQT
     LAALRAPVDA FFDGVMVNAE QPELRRNRLG LLKTLHLAMN RVADLARLAA
//
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