ID W1S0P2_9SPHN Unreviewed; 694 AA.
AC W1S0P2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=C100_17575 {ECO:0000313|EMBL:ETI61579.1};
OS Sphingobium sp. C100.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1207055 {ECO:0000313|EMBL:ETI61579.1, ECO:0000313|Proteomes:UP000018867};
RN [1] {ECO:0000313|EMBL:ETI61579.1, ECO:0000313|Proteomes:UP000018867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C100 {ECO:0000313|EMBL:ETI61579.1,
RC ECO:0000313|Proteomes:UP000018867};
RX PubMed=24482512;
RA Dong C., Bai X., Lai Q., Xie Y., Chen X., Shao Z.;
RT "Draft Genome Sequence of Sphingobium sp. Strain C100, a Polycyclic
RT Aromatic Hydrocarbon-Degrading Bacterium from the Deep-Sea Sediment of the
RT Arctic Ocean.";
RL Genome Announc. 2:0-0(2014).
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:ETI61579.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYOY01000173; ETI61579.1; -; Genomic_DNA.
DR RefSeq; WP_024021047.1; NZ_AYOY01000173.1.
DR AlphaFoldDB; W1S0P2; -.
DR STRING; 1207055.C100_17575; -.
DR PATRIC; fig|1207055.3.peg.3358; -.
DR eggNOG; COG0751; Bacteria.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000018867; 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:UP000018867}.
FT DOMAIN 573..684
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|Pfam:PF05746"
SQ SEQUENCE 694 AA; 75247 MW; 4EB4AFD39F201A24 CRC64;
MTDFLLELRC EEIPARMQLK ASDDLARLFT EELAKSGLTP GRIDSFVTPR RLALIARDLP
RETAAVSEEF KGPRTSAPAQ ALEGFLRKTG LTQDQLEDRE GVWFAVVNKP GRATADVLAQ
AIPAVIRAFP WPKSMRWGGA SQTTESLRWV RPLQGIVAIL GEDLVDVEID GLKSGYATLG
HRFHHPGEIT IGGAHDYVEK LRACHVIASH PERQAIIAAK AAEAAAAHGY SVIEDKWLVA
ENAGLTEWPV PLLGDFDPAF LEVPPEVIQL TLRINQKYFV LRDGDGKLAP AFICTANIEA
KDGGAAIIAG NRKVLAARLS DARFFWEQDK KTRLEEHARK LERITFHEKL GTVADKVERV
ARFAQLLAEH NIVPGCDPAL ARQAAQLCKA DLVTEMVGEF PELQGVMGGY YALAEGLPDA
VADAIRDHYK PIGQGDDVPT APVTVAVSLA DKLDSIWSFF DIDEKPTGSK DPFALRRAVL
GVIQLITVNN LRFSLEQLRL LAERPLFSSQ ATADLSNFFA DRLKVQQKEA GIRHDLIDAV
FALGGEDDLV RLLARVHALQ SFVATDDGVN LLAGYKRAAN ILKKDTGGNI SKTAAANMLI
DGHVAPSPDA PEPAEAALIA ALDAAEPRAA QAVAEERFED AMAALASLRA PIDAFFDAVT
VNDADAGKRA ARLALLARVR DAVQKVADFS KIAG
//