UniProt: A0A0U1KN96

Database: UniProt
Entry: A0A0U1KN96_9BACI

LinkDB:  A0A0U1KN96_9BACI 
Original site:  A0A0U1KN96_9BACI

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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   A0A0U1KN96_9BACI        Unreviewed;       697 AA.
AC   A0A0U1KN96;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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   ECO:0000313|EMBL:CQR46874.1};
GN   ORFNames=BN1058_01157 {ECO:0000313|EMBL:CQR46874.1};
OS   Paraliobacillus sp. PM-2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Paraliobacillus.
OX   NCBI_TaxID=1462524 {ECO:0000313|EMBL:CQR46874.1, ECO:0000313|Proteomes:UP000199066};
RN   [1] {ECO:0000313|EMBL:CQR46874.1, ECO:0000313|Proteomes:UP000199066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM-2 {ECO:0000313|EMBL:CQR46874.1,
RC   ECO:0000313|Proteomes:UP000199066};
RA   Murphy D.;
RL   Submitted (MAR-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|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; CTEI01000001; CQR46874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U1KN96; -.
DR   STRING; 1462524.BN1058_01157; -.
DR   OrthoDB; 9775440at2; -.
DR   Proteomes; UP000199066; 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:UP000199066}.
FT   DOMAIN          584..681
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|Pfam:PF05746"
SQ   SEQUENCE   697 AA;  79421 MW;  C800A2EE22863F30 CRC64;
     MSTTNVLFEI GLEEMPARFL ADTEKQLQQK TTEWLSSIRL SHKNIKTFVT PRRLAVVIEG
     LATKQLDQEE EAKGPAKKIA LDEAGNWSKA AIGFTKGQGK SVDDIYFKEI KGTEYVFVNK
     YIEGSNAEDL LPGFKDVILQ LNFPKNMRWA NKNLRFVRPI RWIVALNNSK VIPFEIASVT
     TSNTTYGHRF LGEEVTISNP LDYQKVLMNQ CVIADSKDRK QLIVEQIEQL ETQKGWHIPK
     DNELLEEVTQ LVEYPTVFFG SFSETYLTIP DEVLITSMKE HQRYFPVMNN NSELLPYFIA
     VRNGDDQHIE LVAKGNEKVL KARLSDAMFF YEEDQKQSIE KNNEKLERMV FQEKLGTIAD
     KVKRVVTLTD KLTELLEIDD VTKQHAIRAA QISKFDLVTN MVNEFTKLQG IMGEKYAKIF
     GEDNRVAKAI NEHYMPRSAN DALPTTIEGA IVSIADKLDT IIGCIYVGLI PSGSQDPYAL
     RRQAIGVLQI LQEKDWGISV EDLLKATKEI YQKSDVALES EQITDEQIAS FFYARASFIL
     KEATNEHDII HAVLANGIGN ISFTYKKAEL LAVKKHDPDF KDTQEALVRV LNIAKKGEST
     SVDPSIFENE HEQKLYDIYQ SIKPTFLKQL DAYEAEQSLL TLSELTQSIH TFFDHTMVMA
     DNEEIKQNRI SLLNDIASLI NRYADLSIIE WKQQVSS
//

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