ID A0A259US30_9FIRM Unreviewed; 687 AA.
AC A0A259US30;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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 ECO:0000313|EMBL:OZC20960.1};
GN ORFNames=SPACI_23290 {ECO:0000313|EMBL:OZC20960.1};
OS Sporomusa acidovorans DSM 3132.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=1123286 {ECO:0000313|EMBL:OZC20960.1, ECO:0000313|Proteomes:UP000216052};
RN [1] {ECO:0000313|EMBL:OZC20960.1, ECO:0000313|Proteomes:UP000216052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3132 {ECO:0000313|EMBL:OZC20960.1,
RC ECO:0000313|Proteomes:UP000216052};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Sporomusa acidovorans DSM 3132.";
RL Submitted (FEB-2016) 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:OZC20960.1}.
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DR EMBL; LSLL01000054; OZC20960.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A259US30; -.
DR STRING; 112900.SAMN04488499_1017121; -.
DR Proteomes; UP000216052; 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 SMART; SM00836; DALR_1; 1.
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:UP000216052}.
FT DOMAIN 579..684
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 687 AA; 75901 MW; C848A8C9F6AB2CCB CRC64;
MTKDLLLEIG TEEIPAKFMP DALAQLESTT KAKLTELRIS YGSVRAVGTP RRLAVIAKEV
GISQADKHSE NKGPAVKIAF DQQGAPTKAA LGFARGQGID PAALVVKDGY VYAVVQEVGR
PVAELLPGLL PDIVNSLSFP KNMRWGDLDM RFVRPIRWLV ALFGNEVVPF TLPGVTSGRI
TRGHRFLGQA EIEVNSVEDY FERLSENFVM VDQDVRRRVI KEQIENLAVS RGGTATIDQE
LLEEVVYLVE YPTALCGNFE EKYLALPPEA IITPMREHQR YFPVKNKDGK LLPMFITVRN
GGPEYIDIVR HGNERVLKAR LADARFFFEE DRKLPLENRV EKLKTVIFQE GLGTIYDKAL
RLERLVAGIG QMVGASQNDL TTAQRGAHLA KADLVTGMVC EFTELQGVMG REYAKLSGER
PEVAEAIFEH YLPRFAGDGL PYTMAGRLIS IADKMDNIVA TFSRGLIPTG SQDPYALRRQ
ALGIVHTMIN AQYHVSLTAM AGQTMDLLGI TDQECRTKLT GELQEFFRLR IKNILTEEQL
RYDMIDAVLA AGSDDLYDTW LRAKAIAVEG GTIAMQKAVQ ALVRVGNLAK NAVSETIDTN
LFTAEAEHDL YKAYLEAKTI ISSYQAEKNY QGVLTAVAAM AAPIDAFFGA VMVMVEEPAV
KNNRLALLKA IAGLAAQTAD LTKIMVM
//
