GenomeNet

Database: UniProt
Entry: I7LE97_9LACO
LinkDB: I7LE97_9LACO
Original site: I7LE97_9LACO 
ID   I7LE97_9LACO            Unreviewed;       305 AA.
AC   I7LE97;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
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   ORFNames=BN53_05830 {ECO:0000313|EMBL:CCI85603.1};
OS   Lactobacillus pasteurii DSM 23907 = CRBIP 24.76.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1423790 {ECO:0000313|EMBL:CCI85603.1, ECO:0000313|Proteomes:UP000009311};
RN   [1] {ECO:0000313|EMBL:CCI85603.1, ECO:0000313|Proteomes:UP000009311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRBIP 24.76T {ECO:0000313|Proteomes:UP000009311};
RA   Cousin S., Bouchier C., Loux V., Ma L., Creno S., Bizet C., Clermont D.;
RT   "Draft Genome Sequence of Lactobacillus pasteurii CRBIP 24.76T.";
RL   Submitted (JUN-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:CCI85603.1}.
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; CAKD01000023; CCI85603.1; -; Genomic_DNA.
DR   RefSeq; WP_009560155.1; NZ_CAKD01000023.1.
DR   AlphaFoldDB; I7LE97; -.
DR   STRING; 1423790.BN53_05830; -.
DR   PATRIC; fig|1423790.3.peg.231; -.
DR   eggNOG; COG0752; Bacteria.
DR   OrthoDB; 9802183at2; -.
DR   Proteomes; UP000009311; 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:0016740; F:transferase activity; IEA:UniProt.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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}; Reference proteome {ECO:0000313|Proteomes:UP000009311}.
SQ   SEQUENCE   305 AA;  35042 MW;  2242EC0FAB6FF0D6 CRC64;
     MSDKKLNVQS MIFKLEQFWA SKGCMIMPSY DVEKGAGTMS PYTFLRAVGP EPWAACYVEP
     SRRPADGRYG ENPNRLFQHH QFQVVIKPAP EDIQQYYLDS LKVLGIDPLE HDIRFVEDNW
     ANPSMGCAGV GWEVWLDGME VSQFTYFQVV GELDVKPTMS EITYGVERLA SYIQDVNSVF
     DLEWGNGILY RDIFKQPEYE HSKYAFESSN QEQLLKFFEI YEATAKRLLD QNLVHPAYDY
     ILKCSHTFNL LDAKGAVSVT ERAGYLSRIR NLAHEVAVKF VEEREKRGFP LLKSAEDKKA
     GVEND
//
DBGET integrated database retrieval system