SYWM_SCHPO
ID SYWM_SCHPO Reviewed; 361 AA.
AC O42875;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=msw1 {ECO:0000312|EMBL:CAA15922.1}; ORFNames=SPAC3G9.13c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAA15922.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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:0000250|UniProtKB:P04803};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P04803}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P04803, ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255}.
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DR EMBL; CU329670; CAA15922.1; -; Genomic_DNA.
DR PIR; T11649; T11649.
DR RefSeq; NP_594085.1; NM_001019500.2.
DR AlphaFoldDB; O42875; -.
DR SMR; O42875; -.
DR STRING; 4896.SPAC3G9.13c.1; -.
DR MaxQB; O42875; -.
DR PaxDb; O42875; -.
DR EnsemblFungi; SPAC3G9.13c.1; SPAC3G9.13c.1:pep; SPAC3G9.13c.
DR GeneID; 2543249; -.
DR KEGG; spo:SPAC3G9.13c; -.
DR PomBase; SPAC3G9.13c; msw1.
DR VEuPathDB; FungiDB:SPAC3G9.13c; -.
DR eggNOG; KOG2713; Eukaryota.
DR HOGENOM; CLU_029244_1_3_1; -.
DR InParanoid; O42875; -.
DR OMA; GWGQFKP; -.
DR PhylomeDB; O42875; -.
DR PRO; PR:O42875; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; ISS:PomBase.
DR GO; GO:0070183; P:mitochondrial tryptophanyl-tRNA aminoacylation; 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 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..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 17..361
FT /note="Tryptophan--tRNA ligase, mitochondrial"
FT /id="PRO_0000314631"
FT MOTIF 22..30
FT /note="'HIGH' region"
FT /evidence="ECO:0000255"
FT MOTIF 225..229
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255"
FT BINDING 21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 27..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 165
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 177..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 225..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UGM6"
FT BINDING 228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04803"
SQ SEQUENCE 361 AA; 39870 MW; 7889FCC85731CA72 CRC64;
MAKLPKITSL LPHSRVVSGI QPTGIPHIGN YLGSLKQWVQ LQEEAARTPF SKCFFFVADL
HALTVPQDPL KFRQARLDML AALLAIGINP QKSTLFFQSD VAQHSELAWL LACSTSMGQL
NRMTQWKSKL HLHDHDDLSF LDASATSSTR FNLGLFSYPV LQAADILLYG ATHIPVGKDQ
SQHVELTRSI ARSFNSSYKE KILTVPDIIL NSSSSIMALC QPEKKMSKSD INSKNYILLS
DSTGEIRKKI SRAQTDNIKG ITYGDSNRPG INNLINIFAA ISDSTPSDIA QANASCSNAE
FKEKVSSAII RCLQPISTSF NEWRQNRELL RDIAKKGAEE AVAEASSCMH KLKTLTGLSV
Y
