ID   SYW_MYCLE               Reviewed;         343 AA.
AC   Q49901;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Tryptophanyl-tRNA synthetase;
DE            EC=6.1.1.2;
DE   AltName: Full=Tryptophan--tRNA ligase;
DE            Short=TrpRS;
GN   Name=trpS; OrderedLocusNames=ML0686; ORFNames=L308_C1_147;
OS   Mycobacterium leprae.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=1769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   MEDLINE=21128732; PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- CATALYTIC ACTIVITY: ATP + L-tryptophan + tRNA(Trp) = AMP +
CC       diphosphate + L-tryptophyl-tRNA(Trp).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; U00022; AAA17323.1; -; Genomic_DNA.
DR   EMBL; AL583919; CAC30195.1; -; Genomic_DNA.
DR   PIR; S73024; S73024.
DR   RefSeq; NP_301552.1; -.
DR   HSSP; P00953; 1MAU.
DR   GeneID; 909578; -.
DR   GenomeReviews; AL450380_GR; ML0686.
DR   KEGG; mle:ML0686; -.
DR   NMPDR; fig|272631.1.peg.424; -.
DR   Leproma; ML0686; -.
DR   HOGENOM; Q49901; -.
DR   OMA; Q49901; NKPGVSN.
DR   BioCyc; MLEP272631:ML0686-MON; -.
DR   BRENDA; 6.1.1.2; 808.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00140; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002305; aa-tRNA-synth_Ib.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002306; Trp-tRNA-synth_Ib.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR10055; Trp_tRNA-synt_1b; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01039; TRNASYNTHTRP.
DR   TIGRFAMs; TIGR00233; trpS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    343       Tryptophanyl-tRNA synthetase.
FT                                /FTId=PRO_0000136650.
FT   MOTIF        16     25       "HIGH" region.
FT   MOTIF       205    209       "KMSKS" region.
FT   BINDING     208    208       ATP (By similarity).
SQ   SEQUENCE   343 AA;  37608 MW;  C0CD552AA6B02D88 CRC64;
     MSTATGFSRI FSGVQPTSDS LHLGNALGAI TQWVALQYDH PDEYEAFFCV VDLHAITIAQ
     DPETLWRRTL VTAAQYLALG IDPGRAVVFV QSHVPAHTQL AWVLGCFTGF GQASRMTQFK
     DKALRQGADS TTVGLFTYPV LQAADVLAYD TDLVPVGEDQ RQHLELARDL AQRFNSRFPD
     TFVVPDMFIP KMAAKIYDLA DPTSKMSKSA SSDAGLINLL DDPALSVKKI RAAVTDSERE
     IRYDPEVKPG VSNLLNIQSA VTGVDVDTLV QRYVGHGYGD LKKDTAEAVV EFVSPIKDRV
     DELMADLTEL EVVLAVGAQR AQDVAGKTMQ RVYDRLGFLP QRG
//