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Database: UniProt
Entry: A0A3A3FUH4_9BURK
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Original site: A0A3A3FUH4_9BURK 
ID   A0A3A3FUH4_9BURK        Unreviewed;       694 AA.
AC   A0A3A3FUH4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
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=D3871_13660 {ECO:0000313|EMBL:RJF99453.1};
OS   Noviherbaspirillum saxi.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Noviherbaspirillum.
OX   NCBI_TaxID=2320863 {ECO:0000313|EMBL:RJF99453.1, ECO:0000313|Proteomes:UP000265955};
RN   [1] {ECO:0000313|Proteomes:UP000265955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K1R23-30 {ECO:0000313|Proteomes:UP000265955};
RA   Zhu H.;
RL   Submitted (SEP-2018) 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:RJF99453.1}.
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DR   EMBL; QYUO01000001; RJF99453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A3FUH4; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000265955; 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:UP000265955}.
FT   DOMAIN          586..679
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   694 AA;  75271 MW;  6BDAC84D059F2464 CRC64;
     MTQTLLVELL TEELPPKALA KLGDAFANGI FNGLKSRDFI DADAVATSYA TPRRLAVAIT
     RVRATSPDKS IREKVLPVSV ALDKEGNPAA PLAKKLAALG FPDLNISELE RASDGKAESF
     FYTYTAPGST LQNGLQAALE ETLGKLPIPK LMSYQRPDGE TVQFVRPAHK LIALHGAEIV
     PITTLGLSAG RVTLGHRFLS QGELSIDSAE SYAAVLQEQG KTIPSGSARK EKIRGELLAK
     AGSDKVLMPE SLLDEVTALV EWPVVYECKF EDAFLSVPQE CLILTMQTNQ KYFALTDAAG
     KLRSRFLIVS NIETGNPQHI IGGNERVVRP RLSDAKFFFE QDKKKKLADR LPGLANVVYH
     NKLGTQGQRT ERVKVLAGRI AAALNADVAL AERGALLAKT DLLTDMVGEF PELQGIMGTY
     YARHDGEPDE VALAASEHYQ PRFAGDALPS TATGTVVALA DKLETLVGIW GIGLQPTGDK
     DPFALRRHAL GVLRMLVEKR LPLALSELLG DAAQLFAGNA NFKDPTADVT AFMLDRLRGL
     LRERGYAQNE IEAVVAQNPD RLDNIVERLD AVKAFAALVE AESLAAANKR ITNILKKTEG
     ARNTVQQGLL KEAAEQGLYS AMTQLKPQVD AAFAKGDFAG TLKSLAQLRD NVDSFFNDVM
     VMAEDEQLRN NRIALLSDLH GMMNRVADIS KLAA
//
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