ID   SYDM_SCHPO              Reviewed;         611 AA.
AC   O94242;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Aspartate--tRNA ligase, mitochondrial;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartyl-tRNA synthetase;
DE            Short=AspRS;
DE   Flags: Precursor;
GN   Name=msd1; ORFNames=SPCC736.06;
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]
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]
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-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC         aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC         Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC         ChEBI:CHEBI:456215; EC=6.1.1.12;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type 1 subfamily. {ECO:0000305}.
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DR   EMBL; CU329672; CAA19270.1; -; Genomic_DNA.
DR   PIR; T41563; T41563.
DR   RefSeq; NP_587777.1; NM_001022770.2.
DR   AlphaFoldDB; O94242; -.
DR   SMR; O94242; -.
DR   BioGRID; 275495; 1.
DR   STRING; 4896.SPCC736.06.1; -.
DR   MaxQB; O94242; -.
DR   PaxDb; O94242; -.
DR   EnsemblFungi; SPCC736.06.1; SPCC736.06.1:pep; SPCC736.06.
DR   GeneID; 2538918; -.
DR   KEGG; spo:SPCC736.06; -.
DR   PomBase; SPCC736.06; -.
DR   VEuPathDB; FungiDB:SPCC736.06; -.
DR   eggNOG; KOG2411; Eukaryota.
DR   HOGENOM; CLU_014330_2_1_1; -.
DR   InParanoid; O94242; -.
DR   OMA; DWPLLEW; -.
DR   PhylomeDB; O94242; -.
DR   PRO; PR:O94242; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; ISS:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IBA:GO_Central.
DR   GO; GO:0070146; P:mitochondrial aspartyl-tRNA aminoacylation; ISS:PomBase.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.1360.30; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00044; Asp_tRNA_synth_type1; 1.
DR   InterPro; IPR004364; Aa-tRNA-synt_II.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004524; Asp-tRNA-ligase_1.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR004115; GAD-like_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   PANTHER; PTHR22594:SF5; PTHR22594:SF5; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00459; aspS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 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..30
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000305"
FT   CHAIN           31..611
FT                   /note="Aspartate--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000315952"
FT   REGION          216..219
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         238..240
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         502
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         509
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         554..557
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   611 AA;  69407 MW;  A61059C7DB374E4C CRC64;
     MVLSRLPACL LPLVGTKVSI QGWLVATSRQ VSKSISFHQL RDTHGTILQL LSTDKIILQQ
     KREPLVSSTD FSQQKSTSVM RTLSSIPPES VVQVTGKLQR RPEHDRRPGN EFELHVEDVK
     LLNVAKNLQL FPGDEKPGMR IQLANRHIQL RAPKYNSYLR QRSRLAYQVH SFFNDREFCE
     VETPLLFKST PEGAREFVVP SRLNPGKFYA LPQSPQQYKQ ILMASGIGNY YQIARCFRDE
     DLRFDRQPEF TQIDLEMSFV DKPHEIMEVV EDLLVRLVSF AKGITLAKPF QHITYQHAID
     KYGSDKPDIR FELPLKNITS LLPKQDPLIS TEILVYNDLS HSLSNAESRK LCEAVGENVV
     VTSIREHSQL QTWVKKLPQL RQLPIVAEEL NQKLQIGINS IVFMTNRPKY LVSGTTPLGK
     LRLLLHELLV KKKALPELDK DLLKFVWVVD FPLFSPTEEK NQSITSTHHP FTAPHWDDVH
     LLEKKPLSVR GLHYDIVVNG IELGGGSIRI HNPDIQRFVL KDVLKLPENR YATFEHLIRV
     LSSGCPPHGG IALGFDRLAA LLTNAPGIRE VIAFPKTSSG ADLLIGSPSA IPEEMLKDYN
     VAITRQTQNR N