SYGA_THEMA
ID SYGA_THEMA Reviewed; 286 AA.
AC Q9WY59;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Glycine--tRNA ligase alpha subunit;
DE EC=6.1.1.14;
DE AltName: Full=Glycyl-tRNA synthetase alpha subunit;
DE Short=GlyRS;
GN Name=glyQ; OrderedLocusNames=TM_0216;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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;
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AE000512; AAD35308.1; -; Genomic_DNA.
DR PIR; B72404; B72404.
DR RefSeq; NP_228031.1; NC_000853.1.
DR RefSeq; WP_004082894.1; NZ_CP011107.1.
DR PDB; 1J5W; X-ray; 1.95 A; A/B=1-286.
DR PDBsum; 1J5W; -.
DR AlphaFoldDB; Q9WY59; -.
DR SMR; Q9WY59; -.
DR STRING; 243274.THEMA_03645; -.
DR EnsemblBacteria; AAD35308; AAD35308; TM_0216.
DR KEGG; tma:TM0216; -.
DR eggNOG; COG0752; Bacteria.
DR InParanoid; Q9WY59; -.
DR OMA; SYYQFQV; -.
DR OrthoDB; 676868at2; -.
DR EvolutionaryTrace; Q9WY59; -.
DR Proteomes; UP000008183; 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; Reference proteome.
FT CHAIN 1..286
FT /note="Glycine--tRNA ligase alpha subunit"
FT /id="PRO_0000072877"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:1J5W"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1J5W"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:1J5W"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1J5W"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:1J5W"
FT STRAND 72..83
FT /evidence="ECO:0007829|PDB:1J5W"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:1J5W"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:1J5W"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:1J5W"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1J5W"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:1J5W"
FT STRAND 134..145
FT /evidence="ECO:0007829|PDB:1J5W"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:1J5W"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:1J5W"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1J5W"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1J5W"
FT HELIX 185..201
FT /evidence="ECO:0007829|PDB:1J5W"
FT HELIX 206..225
FT /evidence="ECO:0007829|PDB:1J5W"
FT HELIX 229..248
FT /evidence="ECO:0007829|PDB:1J5W"
FT HELIX 254..279
FT /evidence="ECO:0007829|PDB:1J5W"
SQ SEQUENCE 286 AA; 33540 MW; 9B8061D54B1160F2 CRC64;
MYLQDVIMKL NDFWASKGCL LEQPYDMEVG AGTFHPATFF GSLRKGPWKV AYVQPSRRPT
DGRYGENPNR LQRYFQYQVI IKPSPENSQE LYLESLEYLG INLKEHDIRF VEDNWESPTL
GAWGVGWEVW LDGMEITQFT YFQQIGGISL KDIPLEITYG LERIAMYLQG VDNVYEVQWN
ENVKYGDVFL ENEREFSVFN FEEANVGLLF RHFDEYEKEF YRLVEKNLYL PAYDYILKCS
HTFNLLDARG AISVSQRQTY VKRIQAMARK AARVFLEVQA NENSPA
