SYG_CHLMU
ID SYG_CHLMU Reviewed; 1003 AA.
AC Q9PLC6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 124.
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=glyS; OrderedLocusNames=TC_0178;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39052.1; -; Genomic_DNA.
DR PIR; F81731; F81731.
DR RefSeq; WP_010229721.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PLC6; -.
DR SMR; Q9PLC6; -.
DR STRING; 243161.TC_0178; -.
DR EnsemblBacteria; AAF39052; AAF39052; TC_0178.
DR GeneID; 1246303; -.
DR KEGG; cmu:TC_0178; -.
DR eggNOG; COG0751; Bacteria.
DR eggNOG; COG0752; Bacteria.
DR HOGENOM; CLU_007220_0_0_0; -.
DR OMA; LPIPKRM; -.
DR OrthoDB; 213210at2; -.
DR Proteomes; UP000000800; 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; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
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_0000072888"
FT REGION 1..310
FT /note="Glycine--tRNA ligase alpha subunit"
FT REGION 311..1003
FT /note="Glycine--tRNA ligase beta subunit"
SQ SEQUENCE 1003 AA; 112848 MW; 29E2FBDA964FF128 CRC64;
MSSQPLTLQD MMAAILRFWS EQGCIIHQGY DLEVGAGTFN PATFLQALGP EPFKTAYIEP
SRRPQDGRYG QHPNRLQKYH QLQVILKPVP ENFLSLYLES LKVIGLNLVD HDIRFVHDDW
ENPTIGAWGL GWEVWLNGME ITQLTYFQAV GSKPLEAISG EITYGVERIA MYLQKKNSVY
DVMWNDSLTY GDITQHAEQA WSQYNFETAN TSMWLKHFED FAAEALATLD KGLPLPAYDF
VIKASHAFNM LDSRGVISVT ERTRYITKIR QLARAVADKY VIWRESLGFP LLKTIPSTPT
VTAKQIPHIC QDEDFLLEIG SEELPAAFVP TGIQQLESLA KKLLADHNIS YNNLEVLGTP
RRLALRIQGL SHLTIRPEAE KKGPPLSLLF EEDGSVSSQG EQFFASHGLS ISHRSALDQS
STICRVRSIK GTDYLFLVIP EERIETAAIL VNELPLLIRS MRFPKKMTWD NGGVEYARPI
RWLVALYGDQ VLPISLGFVS SGNISWGHRQ LDNRQLTIPS SKEYIDILRD ACVIVSQKER
RSIIEQGLQN LTGDQTVAIA PEHLIEETVF LTEHPFVICA QFNPDFCSLP KELLIAEMIN
HQRYFPTQNL QGEITNRFLI VCDNSPTDTI IEGNEKALAP RLTDGNFLFK QDLLTSLDSF
VEKLKSVTYF DALGSLADKT ARLKLHLEET YPLLPLCPKE DIDTAVHYCK ADLVSAVVNE
FPELQGIMGR YYLQNAALSK AAAIAVGEHL QHITLGSSVS TTGALLSILD RVDNLLSCFI
LGLLPTSSHD PYALRRQSLE LLTLLYTTQS SVDIEDLFSR LVRHFPTTIP NTVWSPEDVL
NKLCSFVWGR LKTILSSLGF AKEVIAAVLT ENCPKNPLTI INSARSIQEL QNTQTLETIA
STHNRLKKIL ASLSFSVTEQ IFSLITSEDM LFKQALERFK EATTSLPISS REYLLQLEDL
SQSTALFLDS VRIADDDENI RNQRIALLVA TQKCFGFYAW DAL