ID A0A0U3EWQ2_9BURK Unreviewed; 702 AA.
AC A0A0U3EWQ2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=AT984_15840 {ECO:0000313|EMBL:ALT78439.1};
OS Paucibacter sp. KCTC 42545.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1768242 {ECO:0000313|EMBL:ALT78439.1, ECO:0000313|Proteomes:UP000056576};
RN [1] {ECO:0000313|EMBL:ALT78439.1, ECO:0000313|Proteomes:UP000056576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42545 {ECO:0000313|EMBL:ALT78439.1,
RC ECO:0000313|Proteomes:UP000056576};
RA Kim S.-G., Lee Y.-J.;
RT "Complete genome of Paucibacter sp. KCTC 42545.";
RL Submitted (DEC-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}.
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DR EMBL; CP013692; ALT78439.1; -; Genomic_DNA.
DR RefSeq; WP_058720923.1; NZ_CP013692.1.
DR AlphaFoldDB; A0A0U3EWQ2; -.
DR STRING; 1768242.AT984_15840; -.
DR KEGG; pkt:AT984_15840; -.
DR OrthoDB; 9775440at2; -.
DR Proteomes; UP000056576; 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 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:UP000056576}.
FT DOMAIN 597..700
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 702 AA; 74396 MW; 4DA854A2C3F5561F CRC64;
MSANSKNLLI ELFVEELPPK ALKKLGEAFT QVLVDSLKAQ GLAAADAVAT SFASPRRLGL
HLTHVAAKAA DRAVQQKLMP VSVALDKDGQ PTQALLKRLG GMGLDASAVA QLKRAPDGKA
EALFLDSIQA GATLAEGAQK ALDEALAKLP IPKVMTYQLA DGWSDVKFVR PAHGLVALHG
SELVPLQALG LTAGRETRGH RFEAQVERIT VESADSYATQ LREQGAVIAS YAERRAEIVR
QLNAAAAVQG LSPIEDEALL DEVNSLVERP NVLTCEFEPE FLAVPQECLI LTMKANQKYF
PLLDAAGKLT HKFLVVSNIS PADASAVIGG NERVVRPRLS DAKFFFDQDR KKSLAERVSG
LAKVVYHGKL GTQGERVERV RAIAKAIAAL LGGAELSAQV DQAAHLAKAD LLTDMVGEFP
ELQGIMGGYY ARHDGLGDAV AMAIEDHYKP RFAGDALPRN EAGLVVAMAD KLETLVGMFG
IGQLPTGDKD PFALRRHALG LVRMLSERAG TLSLDALIAA AVPAFGALIQ NPAAPLSDFI
FDRLSGSLRE QGYSAQEVDA VLALRPQSLG DISQRLAAVR AFAALPEAAA LAAANKRIGN
ILKKSEEPVT ASINPALLQE AAEQGLAAAL AKVGPQADQL FTQGDFTASL SALASLRGPV
DAFFDGVMVN AEDAALRANR LGLLKSLHEA MNRVADLARL AV
//
