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Database: UniProt
Entry: A0A102DCW3_9SPHN
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ID   A0A102DCW3_9SPHN        Unreviewed;       679 AA.
AC   A0A102DCW3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=AQZ50_04985 {ECO:0000313|EMBL:KUR79208.1};
OS   Novosphingobium sp. Fuku2-ISO-50.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1739114 {ECO:0000313|EMBL:KUR79208.1, ECO:0000313|Proteomes:UP000056630};
RN   [1] {ECO:0000313|EMBL:KUR79208.1, ECO:0000313|Proteomes:UP000056630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fuku2-ISO-50 {ECO:0000313|EMBL:KUR79208.1,
RC   ECO:0000313|Proteomes:UP000056630};
RA   Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA   Glaeser S.;
RT   "Draft genome sequence of Novosphingobium sp. Fuku2-ISO-50 (=DSM 27930), a
RT   Novosphingobium acidiphilum related species isolated from a surface water
RT   sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL   Submitted (OCT-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}.
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:KUR79208.1}.
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DR   EMBL; LLZR01000007; KUR79208.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A102DCW3; -.
DR   STRING; 1739114.AQZ50_04985; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000056630; 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:UP000056630}.
FT   DOMAIN          573..669
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   679 AA;  73236 MW;  7A8221161097FCD2 CRC64;
     MDCKVSGVDG MSAHFLLELR SEEIPARMQA QARADLERLF RKELESAGLR PGAIPDAVKV
     WSTPRRLALI ARDLPLATEA VREELKGPRT SAPPQALEGF LRKTGLSADQ LTERDGVWFA
     VLERPGRATA DVLAEAIPAL IRAFPWPKSQ RWGAASLSSE SLRWVRPLSG IIALLGGEVV
     PCDIGGIVSG RETVGHRFHH QGTITIDGVD DYAAKLRAAH VIVDHAEREA IVRDGARRAA
     SEAGLVLVDD EGLVIENAGL TEWPVPLLGR FDEAFLAVPP EVIQLTARVN QKYFICRDAA
     GKLANAFVCT ANIAARDEGA AIITGNRKVL AARLSDARFF WDQDQKTPLA EQAKKLGRIT
     FHDKLGSLAE KVARVADLAE WLAQEGLVPG ADPAEARLAA QLCKTDLVTE MVGEFPELQG
     LMGGYYARVE GLPDAVADAI RDHYKPVGQG DDVPRAPVTV AVALADKLDT LRGFFAIDEK
     PTGSKDPFAL RRAALGVIRL ITDNGLRLAV AEGDLLAFFA DRLKVQQREA GVRHDLIDAV
     FALGGEDDLV RLLARVHALQ AFVGTEDGVN LLAGYKRAAN ILKKETWQPL PQTYTAEPDE
     ALLGAALAEA APKVEAGIAS EDFTAAMAAL ASLRAPIDAF FETVTVNDAD ASKRANRLAL
     LDLFRAAVHK VADFSRIEG
//
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