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Database: UniProt
Entry: A0A372BTT8_9GAMM
LinkDB: A0A372BTT8_9GAMM
Original site: A0A372BTT8_9GAMM 
ID   A0A372BTT8_9GAMM        Unreviewed;       693 AA.
AC   A0A372BTT8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-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=DZK25_11290 {ECO:0000313|EMBL:RFF26797.1};
OS   Wenzhouxiangella sp. 15181.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Wenzhouxiangellaceae; Wenzhouxiangella.
OX   NCBI_TaxID=2301224 {ECO:0000313|EMBL:RFF26797.1, ECO:0000313|Proteomes:UP000262558};
RN   [1] {ECO:0000313|EMBL:RFF26797.1, ECO:0000313|Proteomes:UP000262558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=15181 {ECO:0000313|EMBL:RFF26797.1,
RC   ECO:0000313|Proteomes:UP000262558};
RA   Han S.;
RT   "Wenzhouxiangella salilacus sp. nov., a novel bacterium isolated from a
RT   saline lake in Xinjiang Province, China.";
RL   Submitted (AUG-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:RFF26797.1}.
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DR   EMBL; QUZL01000044; RFF26797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372BTT8; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000262558; 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:UP000262558}.
FT   DOMAIN          585..680
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   693 AA;  76101 MW;  8FFB768AF767565B CRC64;
     MSEHADLLIE IGCEELPAGQ LQGQVKLLAQ GLGSRLVDAG LIDSDDDIAQ LGTPRRLAVR
     IPAVRERQAD QVLDRKGPAE NVALDADGNP TKAAEGFARS VGKSFDELEW LENDQGRWLF
     TRVEQPGKSL SELLPEMFDA TVRSMAGARS MRWSDRDDRF LRPVRWLLVL HGEATIELEY
     FGLKADRQTR GHRIHAPGWH AVDSASAYDQ VLEKASVIVD PARRRERIVA QAKRLAGESG
     LMAVLDDALV DEVAGLTEWP VAVMGRFSED FLEVPEEALI SSLEQHQKSF ALRDGEGRLA
     PRFIAVANIE STDPELMTAG FERVIRPRLA DARFFWDQDR RNTLADKRDR LDAILFQEKL
     GSIGDKVRRL ERLVETTAPA LDANIEISAR AAHLCKCDLV TEMVGEFPEL QGIMGRYYAL
     SDGEPKAVAD AIEGHYRPRH AGDELAHDAA GRALALADRL DTVLGVFAAG QKPRGGKDPF
     ALRRAALGIV RLLADSGTTL TIRKALEAAA QPLEGTVAID ETLVDEVEQF VFERLRSWAS
     EQGMETNTVH AVAAGEAGSV ADFLARARAV QQFADDPAMA SLVAANKRAG NLLKQAGLQT
     GQRIDRQLLS EVAESRLAAA IDSTESELDR AMEQADYPAA LATLAKLREP VDAFFDEVMV
     MCDDESLRNN RLALLGHLRA LFLRIADVAR LGR
//
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