SYG_CHLT2
ID SYG_CHLT2 Reviewed; 1003 AA.
AC B0B923; O84802; Q46371;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Glycine--tRNA ligase;
DE AltName: Full=Glycyl-tRNA synthetase;
DE Short=GlyRS;
DE EC=6.1.1.14;
DE Includes:
DE RecName: Full=Glycine--tRNA ligase alpha subunit;
DE AltName: Full=Glycyl-tRNA synthetase alpha subunit;
DE Includes:
DE RecName: Full=Glycine--tRNA ligase beta subunit;
DE AltName: Full=Glycyl-tRNA synthetase beta subunit;
GN Name=glyQS; Synonyms=glyQ, glyS; OrderedLocusNames=CTL0165;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7665503; DOI=10.1128/jb.177.17.5179-5185.1995;
RA Wagar E.A., Giese M.J., Yasin B., Pang M.;
RT "The glycyl-tRNA synthetase of Chlamydia trachomatis.";
RL J. Bacteriol. 177:5179-5185(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
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 -!- 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; U20547; AAA82982.1; -; Genomic_DNA.
DR EMBL; AM884176; CAP03610.1; -; Genomic_DNA.
DR RefSeq; WP_009873412.1; NC_010287.1.
DR RefSeq; YP_001654256.1; NC_010287.1.
DR AlphaFoldDB; B0B923; -.
DR SMR; B0B923; -.
DR EnsemblBacteria; CAP03610; CAP03610; CTL0165.
DR KEGG; ctb:CTL0165; -.
DR PATRIC; fig|471472.4.peg.178; -.
DR HOGENOM; CLU_007220_1_1_0; -.
DR OMA; LPIPKRM; -.
DR Proteomes; UP000000795; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
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:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
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 HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR PANTHER; PTHR30075; PTHR30075; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF02091; tRNA-synt_2e; 1.
DR Pfam; PF02092; tRNA_synt_2f; 1.
DR PRINTS; PR01044; TRNASYNTHGA.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00388; glyQ; 1.
DR TIGRFAMs; TIGR00211; glyS; 1.
DR PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 2.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..1003
FT /note="Glycine--tRNA ligase"
FT /id="PRO_0000391805"
FT REGION 1..310
FT /note="Glycine--tRNA ligase alpha subunit"
FT REGION 311..1003
FT /note="Glycine--tRNA ligase beta subunit"
FT CONFLICT 221
FT /note="F -> S (in Ref. 1; AAA82982)"
FT /evidence="ECO:0000305"
FT CONFLICT 602..618
FT /note="QRYFPTQNMQGEITNRF -> PTVLPNTKYARRNHQSI (in Ref. 1;
FT AAA82982)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="T -> P (in Ref. 1; AAA82982)"
FT /evidence="ECO:0000305"
FT CONFLICT 828
FT /note="S -> SARFAS (in Ref. 1; AAA82982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1003 AA; 112503 MW; C8BA83A0F4CF17B9 CRC64;
MSSQPLTLQA MMAAILNFWS EQGCIIHQGY DLEVGAGTFN PATFLQSLGP EPFRTAYIEP
SRRPQDGRYG QHPNRLQKYH QLQVILKPVP ENFLSLYLES LKVIGLNLVD HDIRFVHDDW
ENPTIGAWGL GWEVWLNGME ITQLTYFQAV GSKPLDAISG EITYGVERIA MYLQKKNSVY
DVMWNGSLTY GDITQYAEQA WSQYNFETAN TTMWLKHFDD FSAEALATLD QGLPLPAYDF
VIKASHAFNM LDSRGVISVT ERTRYIAKIR QLARAAADKY VAWRESLGFP LLKTPPSTPT
VTPKKIPTIC QPEDFLLEIG SEELPATFVP TGIQQLESLA KKLLADHGIA YKHLEVLGTP
RRLALCIEGL SHVTIRPESE KKGPPLSLLF MTDGSVSPQG EQFFPSHGLS ISHRSALDQP
SAICRVRSIN GTDYLFLVIP EERKETAAIL VNELPQLIRS IRFPQKMTWD NGGVEYARPI
RWLVALYGDQ ILPISLGFVS SGNTSWGHRQ LDNRQLTIPS SNMYVDTLRS ACVIVSQKER
RAIIKQGLQN LTGDQIVAIA PEHLVDETVF LTEHPFVISA QFDPAFCSLP KELLIAEMIQ
HQRYFPTQNM QGEITNRFLI VCDNSPTDSI VEGNEKALAP RLTDGNFLFK QDLLTPLSSF
VEKLKSVTYF ESLGSLADKT SRLKLHLEEA YALLPLCAKE DIDTAIHYCK ADLVSSVVNE
FPELQGIMGR YYLQNASLSR AAALAIGEHL QHITLGSNIS TTGALLSILD RIDNLLSCFI
LGLLPTSSHD PYALRRQSLE ILTLLYTTQS SVDIEDLFAR LIRHFPSSIP NTVWSPEEVL
SKLNTFVWGR LRTILSSLGF DKEIIATVLT DNCPKNPLTI IQSAQSIQEL KNTQILKTIA
ATHNRLKKIL ASLSFSVTEQ MFSLQSAEDL LFKQALDRFV EETTALPISS KDYLHLLKEL
AQSTELFLDS VRVASDDEST RNQRIALLIA AQKCFGFYAW DVL
