UniProt: A0A1G5DVF2

Database: UniProt
Entry: A0A1G5DVF2_9PROT

LinkDB:  A0A1G5DVF2_9PROT 
Original site:  A0A1G5DVF2_9PROT

All links

Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (3)   
   Pfam (2)   
   PROSITE (1)   
All databases (14)   

Download RDF

ID   A0A1G5DVF2_9PROT        Unreviewed;       707 AA.
AC   A0A1G5DVF2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=SAMN05216308_105108 {ECO:0000313|EMBL:SCY18537.1};
OS   Nitrosospira sp. Nsp13.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=1855332 {ECO:0000313|EMBL:SCY18537.1, ECO:0000313|Proteomes:UP000198731};
RN   [1] {ECO:0000313|EMBL:SCY18537.1, ECO:0000313|Proteomes:UP000198731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nsp13 {ECO:0000313|EMBL:SCY18537.1,
RC   ECO:0000313|Proteomes:UP000198731};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FMVD01000005; SCY18537.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5DVF2; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000198731; 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}.
FT   DOMAIN          598..697
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   707 AA;  77206 MW;  4A2869FB03F46E0E CRC64;
     MSNATGNLLI ELLVEELPPK SLKKLGDSFA EVIAANLKAQ GLAKNDVVIT AFASPRRLAV
     HIKNVTVQAA DKSASQKLMP VSVGLDSNGQ ATPALLKKLG SLCIDATDMP VSQLKRTFDG
     KVEALFFDSV VKGVVLAEGL QRAIDEALIK LPIARMMTYQ LADGWKSVNF VRPVHGLVAL
     HDAEIIPISV LGLTAGRETQ GHRFEARVKA VMLKNADSYE SQLKNEGAVI ASFPARRAEI
     VRQLQAVSAE TGLQPVEDEA LLDEVTGLVE QPSVLVGKFD NAFLEVPQEC LILTMKANQK
     YFPLLDANGK LSHQFLIVSN IRPADASQII TGNERVLRSR LADAKFFFDQ DRKKTLAARV
     AGLDKVVYHN KIGTQAERVE RIWAIAQAIG LRLGGNELAA QAGEAAMLSK ADLLTGMVGE
     FPELQGIMGR YYAQHDGLSH DIAFAIEDHY KPRFAGDELP RNMTGLCVAL ADKLETLVGM
     FGIGQIPTGD KDPFALRRNA LGVTRMLTEK KLEISLEEII RISSGVFNNK INFGDAESHQ
     LLNFIYERMS SQLREQGYSP QQIEAVIAKR PQFLNEIHQR LAAVRAFSAL PEAESLAAAN
     KRVSNILKKA EGAVSSTVNA TLLREPAEQA LHAALNTIMP KTDIAFKLGK FSLALQELAA
     LKTPVDTFFD KVMVNTEDAD LRANRLALLA QLRQEMNRVA DISKLAT
//

DBGET integrated database retrieval system