SYW_THEMA
ID SYW_THEMA Reviewed; 328 AA.
AC Q9WYW2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Tryptophan--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00140};
DE EC=6.1.1.2 {ECO:0000255|HAMAP-Rule:MF_00140};
DE AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00140};
DE Short=TrpRS {ECO:0000255|HAMAP-Rule:MF_00140};
GN Name=trpS {ECO:0000255|HAMAP-Rule:MF_00140}; OrderedLocusNames=TM_0492;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp).
CC {ECO:0000255|HAMAP-Rule:MF_00140}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00140};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00140}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00140}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00140}.
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DR EMBL; AE000512; AAD35577.1; -; Genomic_DNA.
DR PIR; C72370; C72370.
DR RefSeq; NP_228302.1; NC_000853.1.
DR RefSeq; WP_004081463.1; NZ_CP011107.1.
DR PDB; 2G36; X-ray; 2.50 A; A=1-328.
DR PDBsum; 2G36; -.
DR AlphaFoldDB; Q9WYW2; -.
DR SMR; Q9WYW2; -.
DR STRING; 243274.THEMA_02210; -.
DR EnsemblBacteria; AAD35577; AAD35577; TM_0492.
DR KEGG; tma:TM0492; -.
DR eggNOG; COG0180; Bacteria.
DR InParanoid; Q9WYW2; -.
DR OMA; GWGQFKP; -.
DR OrthoDB; 951354at2; -.
DR EvolutionaryTrace; Q9WYW2; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00806; TrpRS_core; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00140_B; Trp_tRNA_synth_B; 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 InterPro; IPR024109; Trp-tRNA-ligase_bac-type.
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; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..328
FT /note="Tryptophan--tRNA ligase"
FT /id="PRO_0000136699"
FT MOTIF 9..17
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT MOTIF 193..197
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 8..10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 16..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 136
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 148..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT BINDING 193..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00140"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 15..19
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:2G36"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:2G36"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2G36"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 129..138
FT /evidence="ECO:0007829|PDB:2G36"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:2G36"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 152..168
FT /evidence="ECO:0007829|PDB:2G36"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 237..244
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 249..260
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 266..293
FT /evidence="ECO:0007829|PDB:2G36"
FT HELIX 297..323
FT /evidence="ECO:0007829|PDB:2G36"
SQ SEQUENCE 328 AA; 37770 MW; E31EA170720D2857 CRC64;
MRILSGMRPT GKLHIGHLVG ALENWVKLQE EGNECFYFVA DWHALTTHYD DVSKLKEYTR
DLVRGFLACG IDPEKSVIFV QSGVKEHAEL ALLFSMIVSV SRLERVPTYK EIKSELNYKD
LSTAGFLIYP VLQAADILIY KAEGVPVGED QVYHIELTRE IARRFNYLYD EVFPEPEAIL
SRVPKLPGTD GRKMSKSYGN IINLEISEKE LEQTILRMMT DPARVRRSDP GNPENCPVWK
YHQAFDISEE ESKWVWEGCT TASIGCVDCK KLLLKNMKRK LAPIWENFRK IDEDPHYVDD
VIMEGTKKAR EVAAKTMEEV RRAMNLMF
