ID   SYW_METMA               Reviewed;         491 AA.
AC   Q8PWV5;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2002, sequence version 2.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Tryptophan--tRNA ligase;
DE            EC=6.1.1.2;
DE   AltName: Full=Tryptophanyl-tRNA synthetase;
DE            Short=TrpRS;
GN   Name=trpS; OrderedLocusNames=MM_1471;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM31167.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE008384; AAM31167.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8PWV5; -.
DR   SMR; Q8PWV5; -.
DR   KEGG; mma:MM_1471; -.
DR   PATRIC; fig|192952.21.peg.1698; -.
DR   eggNOG; arCOG01887; Archaea.
DR   HOGENOM; CLU_032621_3_0_2; -.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1.
DR   HAMAP; MF_00140_A; Trp_tRNA_synth_A; 1.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002306; Trp-tRNA-ligase.
DR   InterPro; IPR020653; Tryptophan-tRNA-ligase_arc.
DR   PANTHER; PTHR10055:SF1; TRYPTOPHAN--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR10055; TRYPTOPHANYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 2.
DR   PRINTS; PR01039; TRNASYNTHTRP.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..491
FT                   /note="Tryptophan--tRNA ligase"
FT                   /id="PRO_0000136725"
FT   REGION          295..349
FT                   /note="Insert"
FT   MOTIF           74..82
FT                   /note="'HIGH' region"
FT   MOTIF           375..379
FT                   /note="'KMSKS' region"
SQ   SEQUENCE   491 AA;  55728 MW;  D7ADE51A4F4E9D3C CRC64;
     MDNKLDPWSS SNITDYSKLF EEFGISPFEN ILPEIPSPHK YMRRRIIFGH RDYEQIAEAM
     RTGAPFSVMD GFMPSGKVHL GHKMVMDQIV WHQEKGASAF VGIADREAFS VRGFSWQKCR
     EIGVEEYILS LIALGFKPEG LIYFQSGCGS VKDLAFELGA KVNFSELSAI YGFSGETSLS
     HMLSVATQAA DILQPQLEEF GGSKPVVVPV GPDQDPHLRL TRGLAGKMNM FRVEERETAE
     GGKYLSVRGK GAPREALQEL KKRIPGKVKL YEEHIDVLQT PDYAFLERFV LQINQPERRN
     YFMTQIQEIA TFANAAKPPE FSEYEKYFVF KRVWKTTGKI LEEVVAEVAA EFDGYAFIPP
     ASTYHRFMSG LQGGKMSSSI PDSHIALTDD PKEGAKKVKR AKTGGCITLE EQKKLGGKPD
     ECSVFELMLF HLIEDDEELL EIREECIYGT RMCGSCKQLA AEKMQEFLKD HQEKRELARE
     QLDEYRIIYK K
//