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Database: UniProt
Entry: A0A0X8GPW3_9BURK
LinkDB: A0A0X8GPW3_9BURK
Original site: A0A0X8GPW3_9BURK 
ID   A0A0X8GPW3_9BURK        Unreviewed;       690 AA.
AC   A0A0X8GPW3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=VN23_19185 {ECO:0000313|EMBL:AMC36560.1};
OS   Janthinobacterium sp. B9-8.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=1236179 {ECO:0000313|EMBL:AMC36560.1, ECO:0000313|Proteomes:UP000069577};
RN   [1] {ECO:0000313|EMBL:AMC36560.1, ECO:0000313|Proteomes:UP000069577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B9-8 {ECO:0000313|EMBL:AMC36560.1,
RC   ECO:0000313|Proteomes:UP000069577};
RA   Xu X., Jin W., Wu Q., Jiang L., Huang H.;
RT   "The whole genome sequence of Janthinbacterium sp. B9-8, a bacterium
RT   isolated from low temperature sewage.";
RL   Submitted (JAN-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|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}.
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DR   EMBL; CP014222; AMC36560.1; -; Genomic_DNA.
DR   RefSeq; WP_046351760.1; NZ_CP014222.1.
DR   AlphaFoldDB; A0A0X8GPW3; -.
DR   STRING; 1236179.VN23_19185; -.
DR   KEGG; jab:VN23_19185; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000069577; Chromosome.
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}.
FT   DOMAIN          582..681
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   690 AA;  74339 MW;  00B0AA54AC587E0D CRC64;
     MSNLVSQTLL IEIFTEELPP KALPKLGAVF ASGIFDELVK LGFVAKDAEV ESFASPRRLA
     VSIANVLAVQ PDQAIERRGP AVASGLKDGV PTPALAGFAR SCGVDVAQLA QGSDGKQDVY
     IFSSVKTGEA LTKVLSGIIA ATLKKLPAPK MMRWGDRDGQ FIRPVHGLVV LHGDDVVPAQ
     FLHLEAGRST LGHRFLSSGE IELANADEYA ARLFDDGFVE ASFDARRALI ADQLKNACTE
     LNAQIAPSDG LLDEVTALVE WPVVYTGNFD EKFLDVPQEC LILSMQQHQK YFPLLDQNGK
     LLPKFLVVSN LETPDPSHII HGNERVLRAR LSDAEFFFEQ DKKKKLESRV PQLANVVYHN
     KIGSQFERVE RLQKIAGAIA VKLNANVADC KRAAYLAKAD LIADMVGEFP ELQGVMGMYY
     ARIDGENEAV ANAIEGHYHP RFAGDTLPVG AVAQAVSLAD KLESIVGIYG IGLIPTGDKD
     PFALRRAALG VLRMVLDLPL DLKELLSITA EAFPAGVVAD GTVEGVYGFM QDRLKNYLAA
     DYPAADIDAV LALNPTLLNE MVIRLQAVAA FKALPEATAL AAANKRIRNI LKKVEGDLPE
     LNAALLSDAA EIALHAELLK LQPVVSSALA SQDFTGALKA LSALKEPVDA FFDSVMVMAE
     DLAVRGNRQA LLAALASLMN RVAELSLLAE
//
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