ID A0A0Q3WNZ6_BRECH Unreviewed; 689 AA.
AC A0A0Q3WNZ6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=AN963_04090 {ECO:0000313|EMBL:KQL48979.1};
OS Brevibacillus choshinensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=54911 {ECO:0000313|EMBL:KQL48979.1, ECO:0000313|Proteomes:UP000051063};
RN [1] {ECO:0000313|EMBL:KQL48979.1, ECO:0000313|Proteomes:UP000051063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8552 {ECO:0000313|EMBL:KQL48979.1,
RC ECO:0000313|Proteomes:UP000051063};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (SEP-2015) 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|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:KQL48979.1}.
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DR EMBL; LJJB01000007; KQL48979.1; -; Genomic_DNA.
DR RefSeq; WP_055743275.1; NZ_LJJB01000007.1.
DR AlphaFoldDB; A0A0Q3WNZ6; -.
DR STRING; 54911.AN963_04090; -.
DR PATRIC; fig|54911.3.peg.4935; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000051063; 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 586..674
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 689 AA; 77532 MW; 8444AE6F4323C3C5 CRC64;
MSKRDLLLEV GLEEMPARFV ASAAAQLKEK VEKWLAAERI PFEQITSMES PRRFAVLIDG
LAEKQPDRND EAKGPARKIA QDDAGNWSKA ALGFARSNGV EPDQLYFKDV NGVEYVHARK
SEVGKATKDL LPQLAETIAG MNFPKNMRWG ANDLKYVRPI RWMVALFGEE LIDLEIAGVK
SGRITRGHRF LGTEVEINHP AEYASKLAEQ HVMVNPDERR ATIVEQIRRM EQENGWKIPM
DEGLLDEVVH LVEYPTALYG TFEEEFLTIP REVLVTSMRE HQRYFPVENA QGQLLNHFVT
VRNGDARALE NVAKGNEKVL RARLSDARFF YVEDQKLPID SCLKRLETIV FHEELGTIGD
KVRRVRKTAS QIAEKLGVSQ EEAKQVDRIA EIAKFDLVTN MVGEFPELQG IMGEDYARKA
GENDVVASGV FEHYLPRFAG DQTPKSAQGA IVSLADKLDT IVGIFSIGIV PTGSQDPYGL
RRMAAGIVTI LLERNWHLSL EQLWDATLET YTAQGVNKRT VEEVKKDLVD FFALRLKNVL
QENGVRYDVV DAVLSSEMSY VPEMMAKAKA LMTAVGDEDF KLIVEQFTRV NNLAQKAEAN
AVDEALFVEE VERSLYQAYL SVQQEVDSLA DQAKALATLA TLREPIQSFF DQVMVMAEDQ
AVRANRLGLL LRLSRLIFAY ADFSKVVFA
//
