ID A0A1F5AL75_9BACT Unreviewed; 694 AA.
AC A0A1F5AL75;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=A2Y69_06130 {ECO:0000313|EMBL:OGD18817.1};
OS Candidatus Aminicenantes bacterium RBG_13_59_9.
OC Bacteria; Candidatus Aminicenantes.
OX NCBI_TaxID=1797268 {ECO:0000313|EMBL:OGD18817.1, ECO:0000313|Proteomes:UP000177868};
RN [1] {ECO:0000313|EMBL:OGD18817.1, ECO:0000313|Proteomes:UP000177868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGD18817.1}.
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DR EMBL; MEXW01000199; OGD18817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5AL75; -.
DR Proteomes; UP000177868; 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 582..677
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 694 AA; 78035 MW; F742A65188F2C52D CRC64;
MEFLLEINTE EMPASHIKSG LAQLREKLER ELAVNHISCQ SLETQGTCRR LVVIGEFAPA
EEDREEVVIG PPRSAAYAPD GTPTKAATGF ARSQNAEIGE LEIMGTARGE YIGLRKKTKG
RATGEVLAAS LPAMITSLSF PKMMKWGEVN LRFSRPIKRI LCLWGGKLLR FSIEGFQTQA
KTSGHRLLAP REFRIRSVGE YETGLRENSV ILSAEKRKSL ILKQVGKRLR PLAADLYPDD
DLLEKLTYDV ELPYVFLGEF PHGYLRLPLE VLSVAMREGQ KLFSVVREGR QIPYFLGVAD
ARGDRKSLIR RGNERVLKAR LEDARFFWEQ DLKVPLTARA EGLKQVTFQE KLGHYGEKSE
RLKHLVAFLY DRLEEKSREG EALQAAALCK VDLLTDMVRE FPSLQGKMGG LYAREEGYPP
AVWQAIYEHY QPAGLEDPLP ASELGALLSL ADKLDSLVGI VGVGIQVTGS SDPFGLRRQA
HGICRIILER KLRLSLDDLA EKAVSNYGDI LVKPKKEILE LCRAFFGQRL RFIFEGQGFR
YDLVGASLGA GSDFPHFSYL RLRALESLQK SPDFEPFILM AKRVNNILRG LPPYVMNPDL
LAENQEKELW SGFTAIKKRA LQLVAAGDFD QAQSLVFELR APLAALFDHV LVMAEDEKLR
QNRLALLQEI SRLLREIADF SQVVVEGEKK EKAI
//
