ID A0A0Q4LML7_9SPHN Unreviewed; 733 AA.
AC A0A0Q4LML7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=ASE97_12165 {ECO:0000313|EMBL:KQN36499.1};
OS Sphingomonas sp. Leaf42.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736219 {ECO:0000313|EMBL:KQN36499.1, ECO:0000313|Proteomes:UP000051880};
RN [1] {ECO:0000313|EMBL:KQN36499.1, ECO:0000313|Proteomes:UP000051880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf42 {ECO:0000313|EMBL:KQN36499.1,
RC ECO:0000313|Proteomes:UP000051880};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN36499.1, ECO:0000313|Proteomes:UP000051880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf42 {ECO:0000313|EMBL:KQN36499.1,
RC ECO:0000313|Proteomes:UP000051880};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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|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:KQN36499.1}.
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DR EMBL; LMLF01000007; KQN36499.1; -; Genomic_DNA.
DR RefSeq; WP_055760881.1; NZ_LMLF01000007.1.
DR AlphaFoldDB; A0A0Q4LML7; -.
DR PATRIC; fig|1736219.3.peg.2587; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000051880; 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; 2.
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; 2.
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:UP000051880}.
FT DOMAIN 625..722
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
FT REGION 378..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 77578 MW; 6BC3A841452A78CB CRC64;
MSDFLLELRS EEIPARMQAR AREDLAKLFV AELGKAGIAA PRVTTYATPR RLVLIAHDLP
EATQAVREEV KGPRASAPPQ ALEGFLRKTG LTREALTERD GVLFAVTEVP GRRTADVLGA
AIPAIVRAFP WPKSMRWGAV SLSPESPRWV RPLQGIVALF GSDVVPCEVA GVSSGATTLG
HRFHHPGSIT IGSAGDYVEK LRACHVIVDQ DERAAIIAVG AKMAARGAGL ELVEDEGLLA
ENAGLTEWPV PLIGRFDAAY LAVPPEVIQL TARVNQKYFV CRDGEGRLAN AFVCTANIDA
ADGGERIVAG NAKVLAARLS DAKFFYETDL RTPLDALLPK LEKIVFHEKL GTVADKVERV
AKLARWLVES GVIKPSPLEG RGLGEGTSST SSAALVDTPL SPTSSGSTAP RAVEVVPGAQ
PTRNSPEGER EALAVMAERA ARLAKADLVT GMVGEFPELQ GLMGGYYAAA QGEDPQVAEA
VRDHYKPVGQ GDDVPVAPVT VAVALADKLD SIVQFFAVGL KPSGSKDPFA LRRSALGILS
LVLDNGVRLP LGKAADVAGH GTGAQDVIDF FADRLKVQQR EAGVRHDLID AVFALGGEDD
LVRLLARVHA LQRFVTTEDG ANLLAGYKRA ANILKKEGPV EGEVARDYTP EPAEAALIAA
LDAAEPRAAA AIAGERFEEA MAALASLRAP IDAFFTEVTV NDADPAKRAA RLALLARVRG
AVHSVADFAK IEG
//
