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Database: UniProt
Entry: E3CYU3_9BACT
LinkDB: E3CYU3_9BACT
Original site: E3CYU3_9BACT 
ID   E3CYU3_9BACT            Unreviewed;       302 AA.
AC   E3CYU3;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
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=Apau_1297 {ECO:0000313|EMBL:EFQ23721.1};
OS   Aminomonas paucivorans DSM 12260.
OC   Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC   Aminomonas.
OX   NCBI_TaxID=584708 {ECO:0000313|EMBL:EFQ23721.1, ECO:0000313|Proteomes:UP000005096};
RN   [1] {ECO:0000313|EMBL:EFQ23721.1, ECO:0000313|Proteomes:UP000005096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12260 {ECO:0000313|EMBL:EFQ23721.1,
RC   ECO:0000313|Proteomes:UP000005096};
RX   PubMed=21304733;
RA   Pitluck S., Yasawong M., Held B., Lapidus A., Nolan M., Copeland A.,
RA   Lucas S., Del Rio T.G., Tice H., Cheng J.F., Chertkov O., Goodwin L.,
RA   Tapia R., Han C., Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Pukall R., Spring S., Rohde M., Sikorski J., Goker M.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Non-contiguous finished genome sequence of Aminomonas paucivorans type
RT   strain (GLU-3).";
RL   Stand. Genomic Sci. 3:285-293(2010).
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}.
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DR   EMBL; CM001022; EFQ23721.1; -; Genomic_DNA.
DR   RefSeq; WP_006300923.1; NZ_CM001022.1.
DR   AlphaFoldDB; E3CYU3; -.
DR   STRING; 584708.Apau_1297; -.
DR   PaxDb; 584708-Apau_1297; -.
DR   eggNOG; COG0752; Bacteria.
DR   HOGENOM; CLU_057066_1_0_0; -.
DR   OrthoDB; 9802183at2; -.
DR   Proteomes; UP000005096; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000005096}.
SQ   SEQUENCE   302 AA;  34813 MW;  6AE4A6132D220300 CRC64;
     MNFQEIVMRL ERFWAEQGCI IQQPYDIEVG AGTMNPATTL RVLGPEPWRV AYVEPSRRPT
     DGRYGENPNR LQHYYQYQVI MQPAPEEIQE IYLDSLRALG IDPAEHDIRF VEDDWESPTI
     GAWGLGWEVW LDGMEVTQFT YFQQVGGIDM ESVPAEITYG LERIAMFVQK VDNVYDLQWV
     GDVKYGDVHH RGEVEHSTYN FDVSDAARLF ELFSHYEQEA RHILDAGLVL PAYDYVLKCS
     HTFNLLDARS AISVTERTGY IGRVRALAGA CCKAYAAQRE AMGYPLMDRF RFADQENRGS
     RR
//
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