ID   SYW_CLOLO               Reviewed;         341 AA.
AC   Q46127;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 48.
DE   RecName: Full=Tryptophanyl-tRNA synthetase;
DE            EC=6.1.1.2;
DE   AltName: Full=Tryptophan--tRNA ligase;
DE            Short=TrpRS;
GN   Name=trpS; Synonyms=trsA;
OS   Clostridium longisporum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B6405;
RA   Brown G.D., Thomson J.A.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L49336; AAC05711.1; -; Genomic_DNA.
DR   HSSP; P00953; 1I6M.
DR   BRENDA; 6.1.1.2; 308341.
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; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    341       Tryptophanyl-tRNA synthetase.
FT                                /FTId=PRO_0000136622.
FT   MOTIF        12     20       "HIGH" region.
FT   MOTIF       201    205       "KMSKS" region.
FT   BINDING     204    204       ATP (By similarity).
SQ   SEQUENCE   341 AA;  38256 MW;  692C820F5A08E4D1 CRC64;
     MAKEIILTGD RPTGKLHIGH YVGSLKNRVQ LQNSGDYRSF IMIADQQALT DNARNPEKIR
     NSLIEVALDY LAVGIDPLKS TILVQSQIPE LNELTMHYLN LVTLSRLERN PTVKAEIKQK
     NFENSIPAGF LIYPVSQAAD ITAFKATTVP VGEDQLPMIE QAREIVRSFN TIYGKEVLVE
     PKAVIPKGTI GRLPGTDGKA KMSKSIGNAI YLADEADVIK QKVMSMYTDP NHIKVTDPGQ
     VEGNTVFTYL DTFCKDTETL EEMKAHYSRG GLGDVKVKKF LNEILQAELE PIRNRRKEFQ
     KDIPEVYRIL KEGSEKAREV AAGTLKEVRE TIGIEYFNNI F
//