UniProt: A0A1I7K742

Database: UniProt
Entry: A0A1I7K742_9BURK

LinkDB:  A0A1I7K742_9BURK 
Original site:  A0A1I7K742_9BURK

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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)   

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ID   A0A1I7K742_9BURK        Unreviewed;       708 AA.
AC   A0A1I7K742;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-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=SAMN05216350_108221 {ECO:0000313|EMBL:SFU93255.1};
OS   Polaromonas sp. YR568.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1855301 {ECO:0000313|EMBL:SFU93255.1, ECO:0000313|Proteomes:UP000217451};
RN   [1] {ECO:0000313|EMBL:SFU93255.1, ECO:0000313|Proteomes:UP000217451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR568 {ECO:0000313|EMBL:SFU93255.1,
RC   ECO:0000313|Proteomes:UP000217451};
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; FPBM01000008; SFU93255.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I7K742; -.
DR   STRING; 1855301.SAMN05216350_108221; -.
DR   Proteomes; UP000217451; 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          600..699
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   708 AA;  75513 MW;  AA0594007E2983DC CRC64;
     MTTQNLLVEL FVEELPPKAL KKLGDAFAGV LFEQLKAQGL TAADSVLTAF ASPRRLAAHV
     TAVAADAADK AVSQKLMPVA VGLDASGNAT PALLKKLQAL GADASAVAGL KRAPDGKAEV
     LFYDSTVKGA TLVEGLQKAV LEAIAKLPID KRMTYQLADG WSDVKFVRPA HGLVALHGSS
     VVAIEALGLK AGNSTHGHRF EASVDPVVLK DADSYAAALQ KDGAVIASFA ARKAEIVKQL
     AAAAAKVGGG VKAIDDDALL DEVTALVERP NVLVCEFEKE FLGVPQECLI LTMKANQKYF
     PLLDASGKLT NKFLVVSNIS PTDASAVIGG NERVVRPRLA DAKFFFDQDR KKALESRVES
     LGKVVYHNKL GTQLQRIGRV RWVAATLAGR LNPAIVPLVV QAATLSKADL TTDMVGEFPE
     LQGVMGRYYA LSDSLSADVA DAIEDHYKPR FSGDSLPRHL VGTVVALADK MVTLVDMFGI
     GQLPTGDKDP YALRRQALGV IRILVERDLP IGVRELISAA EAAWLSAEAQ NVHSLLATMP
     EQLADFIYDR LAGSLREQGY SAQEVDAVLA LRPQRLGDVT KRLAAVRTFA ALPEAAALAA
     ANKRIGNILK KSSDKPSQVD LHLLPEAAEL ALYQAMQTLQ PKADKQFEEG NYTGSLQTLA
     GLRLPVDAFF EGVMVNAEDA TLRAKRLGLL TALHQAMNRV ADLSKLAA
//

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