ID A0A1Y4BT47_9ACTN Unreviewed; 699 AA.
AC A0A1Y4BT47;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-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=B5F84_04820 {ECO:0000313|EMBL:OUO34940.1};
OS Olsenella sp. An290.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=1965625 {ECO:0000313|EMBL:OUO34940.1, ECO:0000313|Proteomes:UP000196134};
RN [1] {ECO:0000313|Proteomes:UP000196134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An290 {ECO:0000313|Proteomes:UP000196134};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUO34940.1}.
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DR EMBL; NFIU01000005; OUO34940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4BT47; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000196134; 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:UP000196134}.
FT DOMAIN 610..685
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 699 AA; 75529 MW; 2804A0FB6763AF2F CRC64;
MAETRDFLLE IGCEEMPSAP LINAVKQLGP LVERGLDEAG LAHGAVRVLS TPRRLAAIVE
GVACQTEAVR EVRRGPAASI AFDEAGAPTR AAEGFARKCG VDASALVRRV DADGREYVFA
ERSEDSRPAL PILSELSERV IGSLEWPNYR SQRWGSEHQT FVRPIRWICA LLGSEVVPVR
YADVTSSNVT RGHRVLGPGE HVVAEPAAYE GVLEAAGVLS EERRRERIAA GIAEVEAERG
GARVDTPRRV LDEVVNLCEW PTVVVGTFDE EFLEVPHEII CESMLSNQRY FPIYDAKGDL
TREFVVVMNT RPENAARVVD GNERVVRARL DDAKFFYEED LRRPLEDYLP RLAEVTFQER
LGTVLDKARR MERLAPVVAT ASLGLDDGRA RLAGRAALLA KADLVTQAVV EFTSQQGVMG
GYYALASGED AEVAEAIRDH YHPRFAGDEP PAGPVGVAVA VADKLDTICG MFAIGQPPTG
SSDPFAVRRS AIGVIAMLRG AAYDALGELV ATSLDALAEQ GIEFDRAETE AAVRTFFQGR
LASIAREEGV SPDTIEAVSA VGVVDPRAFF ARAHALEDAR RAEASVFDDL AQAYARAAHL
SDPSLGTAVD ETLLGDAERA LLAACDEGAA RVAGALAADD FAGALGALAD LKAPIDRFFD
DVLVMDEDTA VRENRLRLLN RFVEVFVGVA DISALTRKK
//
