GenomeNet

Database: UniProt
Entry: Q114P5
LinkDB: Q114P5
Original site: Q114P5 
ID   FMT_TRIEI               Reviewed;         336 AA.
AC   Q114P5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   22-NOV-2017, entry version 73.
DE   RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000255|HAMAP-Rule:MF_00182};
DE            EC=2.1.2.9 {ECO:0000255|HAMAP-Rule:MF_00182};
GN   Name=fmt {ECO:0000255|HAMAP-Rule:MF_00182};
GN   OrderedLocusNames=Tery_1769;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Attaches a formyl group to the free amino group of
CC       methionyl-tRNA(fMet). The formyl group appears to play a dual role
CC       in the initiator identity of N-formylmethionyl-tRNA by promoting
CC       its recognition by IF2 and preventing the misappropriation of this
CC       tRNA by the elongation apparatus. {ECO:0000255|HAMAP-
CC       Rule:MF_00182}.
CC   -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + L-methionyl-
CC       tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).
CC       {ECO:0000255|HAMAP-Rule:MF_00182}.
CC   -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000255|HAMAP-
CC       Rule:MF_00182}.
DR   EMBL; CP000393; ABG51029.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q114P5; -.
DR   SMR; Q114P5; -.
DR   STRING; 203124.Tery_1769; -.
DR   EnsemblBacteria; ABG51029; ABG51029; Tery_1769.
DR   KEGG; ter:Tery_1769; -.
DR   eggNOG; ENOG4105CAE; Bacteria.
DR   eggNOG; COG0223; LUCA.
DR   HOGENOM; HOG000261177; -.
DR   KO; K00604; -.
DR   OMA; LRIVFMG; -.
DR   OrthoDB; POG091H01YM; -.
DR   Proteomes; UP000008878; Chromosome.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.10.25.10; -; 1.
DR   Gene3D; 3.40.50.170; -; 1.
DR   HAMAP; MF_00182; Formyl_trans; 1.
DR   InterPro; IPR005794; Fmt.
DR   InterPro; IPR005793; Formyl_trans_C.
DR   InterPro; IPR037022; Formyl_trans_C_sf.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR   InterPro; IPR001555; GART_AS.
DR   Pfam; PF02911; Formyl_trans_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   SUPFAM; SSF50486; SSF50486; 1.
DR   SUPFAM; SSF53328; SSF53328; 1.
DR   TIGRFAMs; TIGR00460; fmt; 1.
DR   PROSITE; PS00373; GART; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Protein biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN         1    336       Methionyl-tRNA formyltransferase.
FT                                /FTId=PRO_1000020200.
FT   REGION      112    115       Tetrahydrofolate (THF) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00182}.
SQ   SEQUENCE   336 AA;  37076 MW;  E5CAFA7CF39AACFF CRC64;
     MMKIIFFGTP LFAVPTLKKL LDNPKIEVTA VVTQPDKRRG RGNKLIPSPV KSVAVAHNIP
     VWQPRRVKKN PETLNLLREA QADVFVVVAY GQILSTEILE MPKLGCVNVH GSILPKYRGA
     APIQWSIYHG EAETGNTTML MDVGMDTGPM LLKSIIPIGL LDNAVSIAEI LAKDGADLLL
     ETLLRLEDKE IEPIPQDNSL ATYAPLIQNS DYEIDWSRSA LDIHNQIRGF FPNCFTSFRG
     QSLKVMATIP VGTEYWSELP PELQKLEKVW SSESEVVGNI GEVVKVIKGL GPVVQTGSGW
     LLLWQVQLAG KKVVSGWDFA NGTRLLVGEV SEVFSR
//
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