ID   SYWM_DICDI              Reviewed;         377 AA.
AC   Q86A90; Q555V3;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 114.
DE   RecName: Full=Tryptophan--tRNA ligase, mitochondrial;
DE            EC=6.1.1.2;
DE   AltName: Full=Tryptophanyl-tRNA synthetase;
DE            Short=TrpRS;
DE   Flags: Precursor;
GN   Name=wars2; Synonyms=mtrpS; ORFNames=DDB_G0274567;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000012; EAL70176.1; -; Genomic_DNA.
DR   RefSeq; XP_643957.1; XM_638865.1.
DR   AlphaFoldDB; Q86A90; -.
DR   SMR; Q86A90; -.
DR   STRING; 44689.Q86A90; -.
DR   PaxDb; 44689-DDB0231246; -.
DR   EnsemblProtists; EAL70176; EAL70176; DDB_G0274567.
DR   GeneID; 8619385; -.
DR   KEGG; ddi:DDB_G0274567; -.
DR   dictyBase; DDB_G0274567; mtrpS.
DR   eggNOG; KOG2713; Eukaryota.
DR   HOGENOM; CLU_029244_1_4_1; -.
DR   InParanoid; Q86A90; -.
DR   OMA; GWGQFKP; -.
DR   PhylomeDB; Q86A90; -.
DR   PRO; PR:Q86A90; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004830; F:tryptophan-tRNA ligase activity; ISS:dictyBase.
DR   GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; ISS:dictyBase.
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_B; Trp_tRNA_synth_B; 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; IPR024109; Trp-tRNA-ligase_bac-type.
DR   NCBIfam; TIGR00233; trpS; 1.
DR   PANTHER; PTHR43766; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43766:SF1; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00579; tRNA-synt_1b; 2.
DR   PRINTS; PR01039; TRNASYNTHTRP.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 2.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..377
FT                   /note="Tryptophan--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000327720"
FT   MOTIF           22..31
FT                   /note="'HIGH' region"
FT   MOTIF           242..246
FT                   /note="'KMSKS' region"
FT   BINDING         21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT   BINDING         28..31
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT   BINDING         181
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT   BINDING         193..195
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT   BINDING         242..246
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT   BINDING         245
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   377 AA;  42215 MW;  A531E956E586AD18 CRC64;
     MKIDEVNFKD KTKVTVFSGM QPTSSALHLG NYLGAMGNWL KIQDLVTKNN KEEEELLNLS
     ESSSSSSSSQ STKINEKHKL IFSIVDLHSL TSTKSLSPKE LQSNTISVAI NYLACGIDPE
     KVILFNQSMV PAHSELTWIL NCITSFSKLS NMIQFKEKTK SSNEASVSNG LLSYPVLMAA
     DILLYKATHV PVGEDQTQHL EFTRDIAQAF HSNFKSKFFP YPSIITSEQS KRIMSLQDGR
     LKMSKSDPLE ISRISLTDTD DQIKLKIKKS KTDTIIGITY DPINRPDISN LLSIASETSG
     IPITDLQSEF KDKSNAIFKE FLSNSIIKNI SPIREKINYY QSNPKLVRDI LLQGSEKANK
     IANKNLNIIK DIVGLYH
//