SYW_METMA
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 25-MAY-2022, entry version 117.
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};
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DR EMBL; AE008384; AAM31167.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q8PWV5; -.
DR SMR; Q8PWV5; -.
DR STRING; 192952.MM_1471; -.
DR EnsemblBacteria; AAM31167; AAM31167; MM_1471.
DR KEGG; mma:MM_1471; -.
DR PATRIC; fig|192952.21.peg.1698; -.
DR eggNOG; arCOG01887; Archaea.
DR HOGENOM; CLU_032621_3_0_2; -.
DR OMA; SIYHRFM; -.
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; -; 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 Pfam; PF00579; tRNA-synt_1b; 2.
DR PRINTS; PR01039; TRNASYNTHTRP.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
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