ID   FMT_RAT                 Reviewed;         385 AA.
AC   Q5I0C5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Methionyl-tRNA formyltransferase, mitochondrial;
DE            Short=MtFMT;
DE            EC=2.1.2.9 {ECO:0000250|UniProtKB:Q96DP5};
DE   Flags: Precursor;
GN   Name=Mtfmt;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Methionyl-tRNA formyltransferase that formylates methionyl-
CC       tRNA in mitochondria and is crucial for translation initiation.
CC       {ECO:0000250|UniProtKB:Q96DP5}.
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:Q96DP5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24381;
CC         Evidence={ECO:0000250|UniProtKB:Q96DP5};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O77480}.
CC   -!- DOMAIN: Composed of an N- and a C-terminal domain. The N-terminal
CC       domain carries the tetrahydrofolate (THF)-binding site and the C-
CC       terminal domain is presumably involved in positioning the Met-tRNA
CC       substrate for the formylation reaction.
CC   -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000305}.
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DR   EMBL; BC088470; AAH88470.1; -; mRNA.
DR   RefSeq; NP_001009697.1; NM_001009697.1.
DR   AlphaFoldDB; Q5I0C5; -.
DR   SMR; Q5I0C5; -.
DR   STRING; 10116.ENSRNOP00000019671; -.
DR   PaxDb; Q5I0C5; -.
DR   PRIDE; Q5I0C5; -.
DR   GeneID; 315763; -.
DR   KEGG; rno:315763; -.
DR   UCSC; RGD:1309462; rat.
DR   CTD; 123263; -.
DR   RGD; 1309462; Mtfmt.
DR   VEuPathDB; HostDB:ENSRNOG00000014602; -.
DR   eggNOG; KOG3082; Eukaryota.
DR   HOGENOM; CLU_033347_0_0_1; -.
DR   InParanoid; Q5I0C5; -.
DR   OMA; FMPELHA; -.
DR   OrthoDB; 963177at2759; -.
DR   PhylomeDB; Q5I0C5; -.
DR   TreeFam; TF323405; -.
DR   PRO; PR:Q5I0C5; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000014602; Expressed in duodenum and 20 other tissues.
DR   Genevisible; Q5I0C5; RN.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0071951; P:conversion of methionyl-tRNA to N-formyl-methionyl-tRNA; ISS:UniProtKB.
DR   CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR   InterPro; IPR005794; Fmt.
DR   InterPro; IPR005793; Formyl_trans_C.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR041711; Met-tRNA-FMT_N.
DR   Pfam; PF02911; Formyl_trans_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   SUPFAM; SSF53328; SSF53328; 1.
DR   TIGRFAMs; TIGR00460; fmt; 1.
PE   2: Evidence at transcript level;
KW   Mitochondrion; Protein biosynthesis; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..385
FT                   /note="Methionyl-tRNA formyltransferase, mitochondrial"
FT                   /id="PRO_0000010095"
SQ   SEQUENCE   385 AA;  42997 MW;  2CFD3CF0AAABC7F4 CRC64;
     MLLPRRCWGP WLAGRRPRCS CQSPAGFSGK DRRSSRVREK PPWRVLFFGT DHFAREALRA
     LHAARDNKEE KLIEKLEVVT VPSISPKGLP VKQYAIQSQL PVYEWPDMGS GEYDVGVVAS
     FGRLLSEALI LKFPYGILNV HPSCLPRWRG PAPIIHTVLH GDTVTGVTIM QVRPKRFDVG
     PILKQETVAV PPKSTSKELE AVLSKLGANM LISVLKNLPE SLNNGRPQPA EGVTYAPKVS
     AGTSCVKWEE QTSEQVLRLH LAIGDIVPLQ TLWMENTVKL LDLVEVNNSI LADPKVMGQT
     VTPGSVVYHR PSQMLLVHCK DGWIGVRSIM HKKTLTATDF YNGYLHAWYQ KNSHAYPSQC
     KFQTLRLPTK TQQKTKLLLC SALSS