GenomeNet

Database: UniProt
Entry: K2KGT4_HELPX
LinkDB: K2KGT4_HELPX
Original site: K2KGT4_HELPX 
ID   K2KGT4_HELPX            Unreviewed;       298 AA.
AC   K2KGT4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE            EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00254};
DE   AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00254};
DE            Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00254};
GN   Name=glyQ {ECO:0000256|HAMAP-Rule:MF_00254,
GN   ECO:0000313|EMBL:EKE85967.1};
GN   ORFNames=OUI_1131 {ECO:0000313|EMBL:EKE85967.1};
OS   Helicobacter pylori R036d.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1145113 {ECO:0000313|EMBL:EKE85967.1, ECO:0000313|Proteomes:UP000006759};
RN   [1] {ECO:0000313|EMBL:EKE85967.1, ECO:0000313|Proteomes:UP000006759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R036d {ECO:0000313|EMBL:EKE85967.1,
RC   ECO:0000313|Proteomes:UP000006759};
RA   Blanchard T.G., Czinn S.J., McCracken C.M., Abolude K.A., Shefchek K.S.,
RA   Maroo A.M., Santana-Cruz I.S., Tallon L.J., Ficke F.W.F.;
RT   "Comparative Sequence Analysis of H. pylori isolates.";
RL   Submitted (AUG-2012) 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_00254};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00254}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00254}.
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:EKE85967.1}.
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; AMOT01000004; EKE85967.1; -; Genomic_DNA.
DR   RefSeq; WP_001150922.1; NZ_AMOT01000004.1.
DR   AlphaFoldDB; K2KGT4; -.
DR   PATRIC; fig|1145113.3.peg.1108; -.
DR   Proteomes; UP000006759; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00733; GlyRS_alpha_core; 1.
DR   HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR   NCBIfam; TIGR00388; glyQ; 1.
DR   PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02091; tRNA-synt_2e; 1.
DR   PRINTS; PR01044; TRNASYNTHGA.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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_00254};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00254}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00254};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00254};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00254};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00254}.
SQ   SEQUENCE   298 AA;  34371 MW;  9F6848BB02957CEE CRC64;
     MQDFSSLLLK LQEYWKNQGC LVIQPYDIPA GAGTFHPATL LRSLDKKPWN VAYVAPSRRP
     TDGRYGENPN RLGSYYQFQV VIKPSPSNIQ ELYLKSLEVL GINLNEHDIR FVEDNWESPT
     LGAWGLGWEV WLDGMEVTQF TYFQQVGGIA CSPIPVEITY GLERLAMYVQ KVENILEIEW
     AKNNHDSVRY AQVHLESEYE FSKYHFEAAS VTRLLEMFKN AQAEALHCLK NKLPLPAYDL
     VMLCSHFFNV LDARKAISVA ERQNYILQIR DLAKGCALLY KEQEEEREER LKNALTKA
//
DBGET integrated database retrieval system