ID   SYW_ENCCU               Reviewed;         385 AA.
AC   O96771; Q8SQY5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Tryptophan--tRNA ligase;
DE            EC=6.1.1.2;
DE   AltName: Full=Tryptophanyl-tRNA synthetase;
DE            Short=TrpRS;
GN   OrderedLocusNames=ECU11_0530;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-134.
RX   PubMed=9615449; DOI=10.1093/oxfordjournals.molbev.a025971;
RA   Peyretaillade E., Broussolle V., Peyret P., Metenier G., Gouy M.,
RA   Vivares C.P.;
RT   "Microsporidia, amitochondrial protists, possess a 70-kDa heat shock
RT   protein gene of mitochondrial evolutionary origin.";
RL   Mol. Biol. Evol. 15:683-689(1998).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L-
CC         tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671,
CC         Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AL590450; CAD25963.1; -; Genomic_DNA.
DR   EMBL; AJ012470; CAA10034.1; -; Genomic_DNA.
DR   PIR; T43806; T43806.
DR   RefSeq; NP_586359.1; NM_001042192.1.
DR   PDB; 3TZE; X-ray; 2.60 A; A/B=1-385.
DR   PDBsum; 3TZE; -.
DR   AlphaFoldDB; O96771; -.
DR   SMR; O96771; -.
DR   STRING; 284813.O96771; -.
DR   GeneID; 860012; -.
DR   KEGG; ecu:ECU11_0530; -.
DR   VEuPathDB; MicrosporidiaDB:ECU11_0530; -.
DR   HOGENOM; CLU_032621_0_1_1; -.
DR   InParanoid; O96771; -.
DR   OMA; SIYHRFM; -.
DR   OrthoDB; 817008at2759; -.
DR   Proteomes; UP000000819; Chromosome XI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00806; TrpRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002306; Trp-tRNA-ligase.
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   1: Evidence at protein level;
KW   3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..385
FT                   /note="Tryptophan--tRNA ligase"
FT                   /id="PRO_0000136742"
FT   MOTIF           89..98
FT                   /note="'HIGH' region"
FT   MOTIF           268..272
FT                   /note="'KMSKS' region"
FT   HELIX           25..30
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   TURN            31..33
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           39..49
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           55..58
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   STRAND          61..67
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           68..76
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   STRAND          81..87
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           99..112
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   STRAND          116..120
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           122..128
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           133..148
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   TURN            149..151
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           154..156
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   STRAND          157..161
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           162..165
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           166..169
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           170..178
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           182..189
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           197..207
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           208..210
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           212..214
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   STRAND          223..229
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           230..232
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           233..243
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           244..246
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   STRAND          252..256
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           274..276
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           284..294
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           313..315
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           317..325
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           329..340
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           346..370
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           373..380
FT                   /evidence="ECO:0007829|PDB:3TZE"
FT   HELIX           382..384
FT                   /evidence="ECO:0007829|PDB:3TZE"
SQ   SEQUENCE   385 AA;  44189 MW;  2865C3AC95FCC859 CRC64;
     MAEQRITPWD VEVVSTDEVP VAIDYDKIIN QFGCEKFNQA LADRLEKLSG KPAHYFFRRG
     IVFAHRDFNL LLDEIANNRP FYLYTGRGPS SKTMHIGHTI PFLLCKYMQD AFKIRLVIQI
     TDDEKFLWKS MRLEDAMAYG RENIKDIVAL GFDPKLTYIF SNVEASHHFE ENILKISKTI
     NLNEAIKVFG FDMSSNIGQV GFPAKEIAPC FSSSFRFIGK GAMCLVPAAV DQDPFFRLAR
     DKAKALGEKK PSSIYVSLLP DLKGVNRKMS ASDPNSSIYL DDAQDTIRKK IIAYAYSGGR
     KTLEEHREKG GDIDVDVPFE YLKYFLDDDQ ELEKYRSGYI KGEITSKEMK EKCVVVIQEF
     VSRYQESRKR VTDDDLRAFI DINKF