UniProt: A0A1I4NW01

Database: UniProt
Entry: A0A1I4NW01_9PROT

LinkDB:  A0A1I4NW01_9PROT 
Original site:  A0A1I4NW01_9PROT

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (4)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (16)   

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ID   A0A1I4NW01_9PROT        Unreviewed;       735 AA.
AC   A0A1I4NW01;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=SAMN05421880_10934 {ECO:0000313|EMBL:SFM19576.1};
OS   Nitrosomonas nitrosa.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=52442 {ECO:0000313|EMBL:SFM19576.1, ECO:0000313|Proteomes:UP000199561};
RN   [1] {ECO:0000313|EMBL:SFM19576.1, ECO:0000313|Proteomes:UP000199561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm146 {ECO:0000313|EMBL:SFM19576.1,
RC   ECO:0000313|Proteomes:UP000199561};
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}.
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DR   EMBL; FOUF01000009; SFM19576.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4NW01; -.
DR   STRING; 52442.SAMN05421880_10934; -.
DR   Proteomes; UP000199561; 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   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
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   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
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:UP000199561}.
FT   DOMAIN          630..733
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
SQ   SEQUENCE   735 AA;  80780 MW;  07CEAD9AAF8B88BB CRC64;
     MTTKNLLIEL LVEELPPKSL NKLGMHFAES LMNGLKQQHL LQSDAVMTVF ATPRRLAAHI
     TQVLAQASDQ LATTKLMPVS VGLDSEGRAT PALVKKLSSV GVEAFVVSQL GRVKEGKTET
     LFLERKVPGI ALAAGLQKAL DDAIADLPIP KVMSYQLADG WNSVHFIRPA HGLVALHGSE
     IVPVSVLGLT SSKVTQGHRF EASIHPIIIR DTESYAQQLE TEGAVIASFV ERRARIMQQL
     STAAAKENLQ LIQDEALLDE VTALVEHPNV LVGKFPPEFL SVPQECLILT MKANQKYFPL
     LDNEGRLVNT FLIVANICPQ DAHLVVDGNE RVVRSRLADA KFFFEQDLKH TLAARIPGLD
     KVVYHHQLGT QGLRIEYVRA IAHEIGQWLG GNLLAEQAGQ AAQLAKADLL TGMVGEFPEL
     QGVMGRYYAL HEGLGDTIAY AIEDHYKPRF AGDALPRNLV GVCVALADKL ETLINLFGIG
     QVPTGDKDPF ALRRHALGVV RILIEKDLPL ELNQLLKQAI GIVKDERIAQ LWMQRTATAK
     SSVQAEEAGK GLTHRNARSQ ISAEVSDQLI EFIYDRLASN LREQGYSAQE VDAVLALHPQ
     HLNDIPRRLA AVRTFATMPE AESLAAANKR VSNILKKAAE AIPAEVVPER LQAPAERTLY
     QALIEIKDKI EEAFLEKDYT IALQILAELK APIDTFFDHV MVNTDDALLR SNRLALLKAL
     QQAMNRVADI SRLAS
//

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