ID   FMT_SCHPO               Reviewed;         340 AA.
AC   Q9UTG6;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Putative methionyl-tRNA formyltransferase;
DE            EC=2.1.2.9;
GN   Name=fmt1; ORFNames=SPAC1805.09c;
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   -!- FUNCTION: Formylates methionyl-tRNA in mitochondria and the cytoplasm.
CC       Responsible for the formylation of the N-terminally formylated (Nt-
CC       formylated) mitochondrial matrix proteins that are encoded by
CC       mitochondrial DNA. Nt-formylated proteins in the cytoplasm are strongly
CC       up-regulated in stationary phase or upon starvation for specific amino
CC       acids and are targeted for degradation by an E3 ubiquitin ligase-
CC       mediated fMet/N-end rule pathway. Increased Nt-formylation of cytosolic
CC       proteins appears to be important for adaptation to these stresses.
CC       {ECO:0000250|UniProtKB:P32785}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) =
CC         (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-
CC         tRNA(fMet); Xref=Rhea:RHEA:24380, Rhea:RHEA-COMP:9952, Rhea:RHEA-
CC         COMP:9953, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454,
CC         ChEBI:CHEBI:78530, ChEBI:CHEBI:78844; EC=2.1.2.9;
CC         Evidence={ECO:0000250|UniProtKB:P32785};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P32785}.
CC       Mitochondrion matrix {ECO:0000250|UniProtKB:P32785}. Cytoplasm
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB55850.1; -; Genomic_DNA.
DR   PIR; T37894; T37894.
DR   RefSeq; NP_593920.1; NM_001019349.2.
DR   AlphaFoldDB; Q9UTG6; -.
DR   SMR; Q9UTG6; -.
DR   BioGRID; 278762; 10.
DR   STRING; 4896.SPAC1805.09c.1; -.
DR   MaxQB; Q9UTG6; -.
DR   PaxDb; Q9UTG6; -.
DR   EnsemblFungi; SPAC1805.09c.1; SPAC1805.09c.1:pep; SPAC1805.09c.
DR   GeneID; 2542294; -.
DR   KEGG; spo:SPAC1805.09c; -.
DR   PomBase; SPAC1805.09c; fmt1.
DR   VEuPathDB; FungiDB:SPAC1805.09c; -.
DR   eggNOG; KOG3082; Eukaryota.
DR   HOGENOM; CLU_033347_0_0_1; -.
DR   InParanoid; Q9UTG6; -.
DR   OMA; YGGINIH; -.
DR   PhylomeDB; Q9UTG6; -.
DR   PRO; PR:Q9UTG6; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; ISO:PomBase.
DR   GO; GO:0071951; P:conversion of methionyl-tRNA to N-formyl-methionyl-tRNA; IBA:GO_Central.
DR   GO; GO:0070124; P:mitochondrial translational initiation; ISO:PomBase.
DR   CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR   InterPro; IPR005793; Formyl_trans_C.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR   InterPro; IPR041711; Met-tRNA-FMT_N.
DR   Pfam; PF02911; Formyl_trans_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   SUPFAM; SSF50486; SSF50486; 1.
DR   SUPFAM; SSF53328; SSF53328; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Mitochondrion; Protein biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN           1..340
FT                   /note="Putative methionyl-tRNA formyltransferase"
FT                   /id="PRO_0000083096"
SQ   SEQUENCE   340 AA;  38041 MW;  4062187922D4A5CE CRC64;
     MAPKIPLNVI FLGTDEFSIP ILRKLIGCVQ RVRVVSAGGK RQSRRGEIPL PPAAMEANAN
     GLEYIKLQDG WKNFHMRPDD QLAITASFGR FVPFKILNQL PYGGINIHPS LLPKYRGAGP
     VYSTILNGDR LAGVTIQTMD SKQFDKGKSL AQAYLKLNGK ETYTLLTKIL SLGAAGMLEH
     VLLQSLYLPN CQTNTVAPQI HGRITDTGGL QLISKETFPS FQESWAKKIT PEDAHVNFES
     MNTQQIYNMS RAFNHVWCIL NNKKVFLYDV HPLHSTSAED WIHMKPGEFA LLEKNLLLVK
     TLDHVMVIKG GIRLSARKIV DPVEWGKTFN SGRGGRFQYV