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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
 
 
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