SYGA_CAMJJ
ID SYGA_CAMJJ Reviewed; 287 AA.
AC A1VZ59;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Glycine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00254};
DE AltName: Full=Glycyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00254};
DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00254};
GN Name=glyQ {ECO:0000255|HAMAP-Rule:MF_00254};
GN OrderedLocusNames=CJJ81176_0727;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) 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:0000255|HAMAP-Rule:MF_00254};
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00254}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00254}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00254}.
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DR EMBL; CP000538; EAQ72455.1; -; Genomic_DNA.
DR RefSeq; WP_002852069.1; NC_008787.1.
DR PDB; 3RF1; X-ray; 2.20 A; A/B=1-287.
DR PDBsum; 3RF1; -.
DR AlphaFoldDB; A1VZ59; -.
DR SMR; A1VZ59; -.
DR STRING; 354242.CJJ81176_0727; -.
DR EnsemblBacteria; EAQ72455; EAQ72455; CJJ81176_0727.
DR KEGG; cjj:CJJ81176_0727; -.
DR eggNOG; COG0752; Bacteria.
DR HOGENOM; CLU_057066_1_0_7; -.
DR OMA; SYYQFQV; -.
DR Proteomes; UP000000646; 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 Gene3D; 3.30.930.10; -; 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 Pfam; PF02091; tRNA-synt_2e; 1.
DR PRINTS; PR01044; TRNASYNTHGA.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00388; glyQ; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..287
FT /note="Glycine--tRNA ligase alpha subunit"
FT /id="PRO_1000047409"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:3RF1"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:3RF1"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:3RF1"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:3RF1"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:3RF1"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:3RF1"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:3RF1"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3RF1"
FT STRAND 72..83
FT /evidence="ECO:0007829|PDB:3RF1"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:3RF1"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:3RF1"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:3RF1"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:3RF1"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:3RF1"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:3RF1"
FT STRAND 134..145
FT /evidence="ECO:0007829|PDB:3RF1"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:3RF1"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:3RF1"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:3RF1"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:3RF1"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:3RF1"
FT HELIX 189..206
FT /evidence="ECO:0007829|PDB:3RF1"
FT HELIX 210..229
FT /evidence="ECO:0007829|PDB:3RF1"
FT HELIX 233..253
FT /evidence="ECO:0007829|PDB:3RF1"
FT HELIX 258..283
FT /evidence="ECO:0007829|PDB:3RF1"
SQ SEQUENCE 287 AA; 33058 MW; 3ED6803DD5B72908 CRC64;
MTFSQMILNL QNYWQEQGCA IMQPYDMPAG AGTFHPATFL RSLGKKPWAA AYVAPSRRPT
DGRYGENPNR LGAYYQFQVL IKPSPDNIQE LYLKSLENLG FDLKSHDIRF VEDNWESPSL
GAWGLGWEVW LDGMEVTQFT YFQQVGGIAV DLVSAEITYG LERIAMYLQN VDNVYDIVWS
EFNGEKIKYA DVHKQSEYEF SKYNFEVSDV KILNEQFENS YKECKNILEQ GLALPAYDYC
MLAAHTFNLL DARGAISVAQ RQDYMLKIRE LSKNCAEIYK KNLNEAE
