ID   SYMM_SCHPO              Reviewed;         539 AA.
AC   O14000;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Probable methionine--tRNA ligase, mitochondrial;
DE            EC=6.1.1.10;
DE   AltName: Full=Mitochondrial methionyl-tRNA synthetase;
DE            Short=MtMetRS;
DE   Flags: Precursor;
GN   ORFNames=SPAC27E2.06c;
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-methionine + tRNA(Met) = AMP + diphosphate + L-
CC         methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC         Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC         ChEBI:CHEBI:456215; EC=6.1.1.10;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; CU329670; CAB11680.1; -; Genomic_DNA.
DR   PIR; T38454; T38454.
DR   RefSeq; NP_594407.1; NM_001019838.2.
DR   AlphaFoldDB; O14000; -.
DR   SMR; O14000; -.
DR   STRING; 4896.SPAC27E2.06c.1; -.
DR   MaxQB; O14000; -.
DR   PaxDb; O14000; -.
DR   EnsemblFungi; SPAC27E2.06c.1; SPAC27E2.06c.1:pep; SPAC27E2.06c.
DR   GeneID; 2541577; -.
DR   KEGG; spo:SPAC27E2.06c; -.
DR   PomBase; SPAC27E2.06c; -.
DR   VEuPathDB; FungiDB:SPAC27E2.06c; -.
DR   eggNOG; KOG0436; Eukaryota.
DR   HOGENOM; CLU_009710_9_0_1; -.
DR   InParanoid; O14000; -.
DR   OMA; MDTQAFC; -.
DR   PhylomeDB; O14000; -.
DR   PRO; PR:O14000; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; ISS:PomBase.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; ISS:PomBase.
DR   GO; GO:0032543; P:mitochondrial translation; NAS:PomBase.
DR   CDD; cd00814; MetRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR023457; Met-tRNA_synth_2.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR43326; PTHR43326; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   TIGRFAMs; TIGR00398; metG; 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..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..539
FT                   /note="Probable methionine--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000374024"
FT   MOTIF           28..38
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           326..330
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   539 AA;  61946 MW;  AC460BB07E65D463 CRC64;
     MLRKGICRLI HQVSESSKKP YFLTTPIFYV NAAPHLGHLY SLVLTDAIAR FQNLKPDVSV
     ISSTGTDEHG LKVQTVAQTE GVSPLQLCDR NSKRFADLAV AANTKFTHFI RTTNPKHQAS
     VQEFWKTIQK AGMISFERHE GWYCVSDETF YPESAIQKVV DPATKQEKRV SMETGKEVQW
     SSEMNYHFLL SKFQSRLIEH YNKNPNFVQP SIFHTQVLEE LKTGISDLSI SRPKQRLSWG
     IPVPGNSQQT IYVWLDALIN YISVIGYPWL NEKSSLSAGW PANMHVIGKD IIRFHCIYWP
     AFLMAAGLPL PEKILVHSHW TMNKVKMSKS LGNVVDPFWL IEKYGVDTIR YYLLKRGRLT
     SDSNFDIEEL EKDEEHDLRR SLGVLLSRLQ SKKLFISNEI QKQWHKKDDF TEYEDIVHEL
     IELPVVCAQS IDGGCVYEVI NLVQSVLRRV TKLFQLKEPW KLSDDSQEKI DTLMLVAHSL
     RISGILLQPI MPTKSTELLD QLGIPKNQRS LQNATNVFEP TEFTFHSGNN SHLFDKRTQ