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Entry: A0A1Z2TPR8_9EURY
LinkDB: A0A1Z2TPR8_9EURY
Original site: A0A1Z2TPR8_9EURY 
ID   A0A1Z2TPR8_9EURY        Unreviewed;       385 AA.
AC   A0A1Z2TPR8;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=CDI07_09130 {ECO:0000313|EMBL:ASA78452.1};
OS   Thermococcus sp. 5-4.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=2008440 {ECO:0000313|EMBL:ASA78452.1, ECO:0000313|Proteomes:UP000196843};
RN   [1] {ECO:0000313|EMBL:ASA78452.1, ECO:0000313|Proteomes:UP000196843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5-4 {ECO:0000313|EMBL:ASA78452.1,
RC   ECO:0000313|Proteomes:UP000196843};
RX   PubMed=28628615; DOI=10.1371/journal.pgen.1006847;
RA   Cossu M., Badel C., Catchpole R., Daniele G., Marguet E., Barbe V.,
RA   Forterre P., Oberto J.;
RT   "Flipping chromosomes in deep-sea archaea.";
RL   PLoS Genet. 13:e1006847-e1006847(2017).
RN   [2] {ECO:0000313|Proteomes:UP000196843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5-4 {ECO:0000313|Proteomes:UP000196843};
RA   Cossu M., Badel C., Catchpole R., Daniele G., Marguet E., Barbe V.,
RA   Forterre P., Oberto J.;
RT   "Flipping Chromosomes in Deep-Sea Archaea.";
RL   PLoS Genet. 0:0-0(2017).
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; CP021848; ASA78452.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z2TPR8; -.
DR   KEGG; thh:CDI07_09130; -.
DR   OrthoDB; 371821at2157; -.
DR   Proteomes; UP000196843; 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          336..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;  44865 MW;  D589CEDEF0F4A119 CRC64;
     MDDAFKVTPW DVEGMVDYAK LIEEFGTSPL TDELLEKTAR LTRSELPIYF RRRFFFSHRD
     YDKVLADYEN GKGFFLYTGR GPSGPMHIGH IIPFFATKWL QEKFGVNLYV QITDDEKFLF
     KEKLTFDDTK RWAYDNILDI IAVGFDPDKT FIFQDSEFTK IYEMAIPIAK KINYSMAKAV
     FGFTDQSKIG MIFYPAIQAA PTFFERKRCL IPAAIDQDPY WRLQRDFAES LGYYKTAAIH
     SKFVPGLMGL EGKMSASKPE TAVYLTDDPE EAGKKIWKYA LTGGRATAKE QREKGGEPEK
     CVVFKWFEIF FEPDDKKLME RYHACKSGEL LCGQCKRELI ERVQAFLKEH QKKRKEAEKK
     VEKFKYTGEL AREQWDKSIP EPLKN
//
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