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Database: UniProt
Entry: A0A218P366_THECE
LinkDB: A0A218P366_THECE
Original site: A0A218P366_THECE 
ID   A0A218P366_THECE        Unreviewed;       385 AA.
AC   A0A218P366;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Tryptophan--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00140};
DE            EC=6.1.1.2 {ECO:0000256|HAMAP-Rule:MF_00140};
DE   AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00140};
DE            Short=TrpRS {ECO:0000256|HAMAP-Rule:MF_00140};
GN   Name=trpS {ECO:0000256|HAMAP-Rule:MF_00140};
GN   ORFNames=A3L02_07295 {ECO:0000313|EMBL:ASI99373.1};
OS   Thermococcus celer Vu 13 = JCM 8558.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=1293037 {ECO:0000313|EMBL:ASI99373.1, ECO:0000313|Proteomes:UP000197156};
RN   [1] {ECO:0000313|EMBL:ASI99373.1, ECO:0000313|Proteomes:UP000197156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vu 13 {ECO:0000313|EMBL:ASI99373.1,
RC   ECO:0000313|Proteomes:UP000197156};
RA   Oger P.M.;
RT   "Complete genome sequence of Thermococcus celer.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp).
CC       {ECO:0000256|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:0000256|HAMAP-Rule:MF_00140};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00140}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00140,
CC       ECO:0000256|RuleBase:RU363036}.
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DR   EMBL; CP014854; ASI99373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218P366; -.
DR   KEGG; tce:A3L02_07295; -.
DR   OrthoDB; 371821at2157; -.
DR   Proteomes; UP000197156; 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   CDD; cd00806; TrpRS_core; 1.
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; 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; IPR020653; Tryptophan-tRNA-ligase_arc.
DR   NCBIfam; TIGR00233; trpS; 1.
DR   PANTHER; PTHR10055:SF1; TRYPTOPHAN--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR10055; TRYPTOPHANYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   PRINTS; PR01039; TRNASYNTHTRP.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00140};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00140}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00140};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00140};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00140};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00140}.
FT   COILED          340..367
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           82..90
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00140"
FT   MOTIF           253..257
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00140"
SQ   SEQUENCE   385 AA;  45044 MW;  59556FDEBE8EEF32 CRC64;
     MDDGFKVTPW DVEGLVDYNR LIEEFGTSPL TDELLEKTAQ LTKSELPLYF RRRFFFSHRD
     YDKVLADYEN GKGFFLYTGR GPSGPMHIGH IIPFFATKWL QERFGVNLYI QITDDEKFLF
     KERLTFEDTK RWAYDNILDI IAVGFDPDRT FIFQDSEFTK IYEMAIPIAK KINYSMAKAV
     FGFTDQSKIG MIFYPAIQAA PTFFERKRCL IPSAIDQDPY WRLQRDFAES LGYYKTAALH
     SKFVPGLMGL EGKMSASKPE TAIYLTDDPE EAGKKLWKYA LTGGRATAKE QREKGGNPEK
     CVVFKWFEIF FEPDDKKLME RYHACKNGEL LCGQCKRDLI KRVQDFLREH QRRRKEAEKK
     VEKFKYTGEL AREQWDRAIP EALKG
//
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