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Database: UniProt
Entry: D7HH33_VIBCL
LinkDB: D7HH33_VIBCL
Original site: D7HH33_VIBCL 
ID   D7HH33_VIBCL            Unreviewed;       330 AA.
AC   D7HH33;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
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=VCRC385_00025 {ECO:0000313|EMBL:EFH72653.1};
OS   Vibrio cholerae RC385.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345074 {ECO:0000313|EMBL:EFH72653.1, ECO:0000313|Proteomes:UP000004696};
RN   [1] {ECO:0000313|Proteomes:UP000004696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RC385 {ECO:0000313|Proteomes:UP000004696};
RA   Heidelberg J.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFH72653.1, ECO:0000313|Proteomes:UP000004696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RC385 {ECO:0000313|EMBL:EFH72653.1,
RC   ECO:0000313|Proteomes:UP000004696};
RG   The Broad Institute Genome Sequencing Platform;
RA   Colwell R., Grim C.J., Young S., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.,
RA   Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA   Pearson M., Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Walk T., White J., Yandava C., Borodovsky M.,
RA   Heidelberg J., Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Vibrio cholerae RC385.";
RL   Submitted (OCT-2009) 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|ARBA:ARBA00011209, 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}.
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DR   EMBL; GG774563; EFH72653.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7HH33; -.
DR   PATRIC; fig|345074.23.peg.396; -.
DR   HOGENOM; CLU_057066_1_0_6; -.
DR   Proteomes; UP000004696; 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   330 AA;  38103 MW;  7CD79F6ED3F8F0E5 CRC64;
     MSGNIWVYFS VIFYQFRQKN RANLTMQKYD IKTFQGMILA LQDYWAQQGC TIVQPLDMEV
     GAGTSHPMTC LRALGPEPIA TAYVQPSRRP TDGRYGENPN RLQHYYQFQV IIKPSPDNIQ
     ELYLGSLRVL GVDPCVHDIR FVEDNWENPT LGAWGLGWEV WLNGMEVTQF TYFQQVGGLE
     CKPVTGEITY GIERLAMYIQ GVDSVYDLVW TDGPLGKVTY GDIFHQNEVE QSTYNFEHAD
     VDFLFTYFDQ CEKECKYLLE LEKPLPLPAY ERILKAAHAF NLLDARKAIS VTERQRYILR
     IRNLTKSVAE AYYASREALG FPMCKKSEQK
//
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