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Database: UniProt
Entry: A0A418NW25_9SPHN
LinkDB: A0A418NW25_9SPHN
Original site: A0A418NW25_9SPHN 
ID   A0A418NW25_9SPHN        Unreviewed;       719 AA.
AC   A0A418NW25;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, 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=D2V07_00665 {ECO:0000313|EMBL:RIV88824.1};
OS   Aurantiacibacter zhengii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Aurantiacibacter.
OX   NCBI_TaxID=2307003 {ECO:0000313|EMBL:RIV88824.1, ECO:0000313|Proteomes:UP000286576};
RN   [1] {ECO:0000313|EMBL:RIV88824.1, ECO:0000313|Proteomes:UP000286576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V18 {ECO:0000313|EMBL:RIV88824.1,
RC   ECO:0000313|Proteomes:UP000286576};
RA   Fang C., Wu Y.-H., Sun C., Wang H., Cheng H., Meng F.-X., Wang C.-S.,
RA   Xu X.-W.;
RT   "Erythrobacter zhengii sp.nov., a bacterium isolated from deep-sea
RT   sediment.";
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:RIV88824.1}.
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DR   EMBL; QXFL01000001; RIV88824.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418NW25; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000286576; 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:UP000286576}.
FT   DOMAIN          631..711
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   719 AA;  79075 MW;  AA35324CBCD600FF CRC64;
     MSDFLLELRS EEIPARMQAG ARAELEKLFR REMEAAGVDF GDITIWSTPR RLALITRGLP
     DATQPVSSEE KGPPVGAPDQ AVDGFCRKQG VSRDDLEVRD VKGRETYFAV KNIPGRATKD
     LLAEAIPAII RDFSWPKSMR WGEASLSTES LRWVRPLSGI VALLGEELVE CEVHGVTSGW
     VTLGHRFHHS GDITIGSADD YAEKLRACHV IVDHEERQDI VRSAAAKVAA DAGLKLVEDE
     GLVIENAGLT EWPVPLLGRF DEDFLDVPPE VIQLTARVNQ KYFVCEDSAG KLANAFVCTA
     NIEAADGGAA IVDGNRKVLA ARLSDARFFW ELDQKTPLRE HAKKLERITF HEKLGTVADK
     VDRVAKLAAW LTSDARAPNG DHNMARQAAE LSKSDLVTEM VGEFPELQGL MGGYYAEKEG
     LPQEVADAIR DHYKPVGQDD EVPTAPLTVA VSLADKLDNL FSFFNIDILP TGSKDPFALR
     RAALGYLRLV QANGLELSLE QAAQAWGGLG QAKLGTRVAE FLSDRLAVQM REEGVRHDYI
     AASREWQGHT DARTDRIEAR ARALAEFLST DNGTNLLAGY KRAANILKKE DWRGIEGEIA
     RTGEEDPLAL VDDPDMKAVI DAKMSERHAR ELSYTPEPAE KALIEALDAA EPRASQAIEK
     EDFATAMSAL ASLRAPIDAF FEEVTVNDPD EDKRASRLDL LARFRAAVHN VADFSKIEG
//
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