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Database: UniProt
Entry: W1S0P2_9SPHN
LinkDB: W1S0P2_9SPHN
Original site: W1S0P2_9SPHN 
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}.
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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
//
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