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Database: UniProt
Entry: K1NAB3_9LACO
LinkDB: K1NAB3_9LACO
Original site: K1NAB3_9LACO 
ID   K1NAB3_9LACO            Unreviewed;       305 AA.
AC   K1NAB3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-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=HMPREF9249_01623 {ECO:0000313|EMBL:EKB65164.1};
OS   Lactobacillus crispatus FB077-07.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=883092 {ECO:0000313|EMBL:EKB65164.1, ECO:0000313|Proteomes:UP000004722};
RN   [1] {ECO:0000313|EMBL:EKB65164.1, ECO:0000313|Proteomes:UP000004722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB077-07 {ECO:0000313|EMBL:EKB65164.1,
RC   ECO:0000313|Proteomes:UP000004722};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lactobacillus crispatus FB077-07.";
RL   Submitted (JUL-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:EKB65164.1}.
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DR   EMBL; AGZG01000088; EKB65164.1; -; Genomic_DNA.
DR   RefSeq; WP_005719721.1; NZ_JH932273.1.
DR   AlphaFoldDB; K1NAB3; -.
DR   GeneID; 69823587; -.
DR   PATRIC; fig|883092.3.peg.1619; -.
DR   HOGENOM; CLU_057066_1_0_9; -.
DR   OrthoDB; 9802183at2; -.
DR   Proteomes; UP000004722; 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}.
SQ   SEQUENCE   305 AA;  35080 MW;  936D0AD193ADEE01 CRC64;
     MADKKLNIQN MIFKLEQFWS SKGCMIMPSY DVEKGAGTMS PYTFLRAVGP EPWAACYVEP
     SRRPADGRYG ENPNRLFQHH QFQVVIKPAP KDIQQYYLDS LKVLGIDPLE HDIRFVEDNW
     ANPSMGCAGV GWEVWLDGME VSQFTYFQVV GELDVKPTMS EITYGVERLA SYIQDVNSVF
     DLEWGNGILY RDIFKQPEYE HSKYAFEESN QEQLLQFFDI YEATAKRLLD KNLVHPAYDY
     ILKCSHTFNL LDARGAVSVT ERAGYLSRIR NLAHEVAVKF VEEREKRGFP LLKSAEDKKA
     GVENG
//
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