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Q9D799 (FMT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionyl-tRNA formyltransferase, mitochondrial

Short name=MtFMT
EC=2.1.2.9
Gene names
Name:Mtfmt
Synonyms:Fmt
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Formylates methionyl-tRNA in mitochondria. A single tRNA(Met) gene gives rise to both an initiator and an elongator species via an unknown mechanism By similarity.

Catalytic activity

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).

Subcellular location

Mitochondrion By similarity.

Domain

Composed of an N- and a C-terminal domain. The N-terminal domain carries the tetrahydrofolate (THF)-binding site and the C-terminal domain is presumably involved in positioning the Met-tRNA substrate for the formylation reaction.

Sequence similarities

Belongs to the Fmt family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentmitochondrion

Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI

   Molecular_functionmethionyl-tRNA formyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 386Methionyl-tRNA formyltransferase, mitochondrialPRO_0000010094

Experimental info

Sequence conflict401K → M in BAB26282. Ref.1
Sequence conflict3051F → S in AAH19509. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9D799 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 74B0542C0ECA4D9D

FASTA38643,092
        10         20         30         40         50         60 
MLLPRCCWGR WLMGRRPRCS CQAPAGFDGK DGRGSRVREK PPWRVLFLGT DHFARETLRA 

        70         80         90        100        110        120 
LHAARDGKEE KLIEKLEVVT VPSLSPKGLP VKQYAIQSQL PVYEWPDVGS GEYDVGVVAS 

       130        140        150        160        170        180 
FGRLLSEALI LKFPYGILNV HPSCLPRWRG PAPIIHTVLH GDTVTGVTIM QIRPKRFDIG 

       190        200        210        220        230        240 
PILQQETIPV PPKSTSKELE AVLSKLGANM LISVLKNLPE SLNNGRPQPA EGVTYAPKVS 

       250        260        270        280        290        300 
AGTSCVKWEE QTSEQVLRLH LAIGDIVPLQ TLWMENTVKL LDLVEVNNSI LADPKLTGQT 

       310        320        330        340        350        360 
VTPGFVVYHR PSQMLLVRCK DGWIGVRSVM LKKTLTATDF YNGYLHAWYQ KNSHAHPSQC 

       370        380 
RFQTLRLPTK MQQKTKLLLC NSALSS 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Tongue.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK009430 mRNA. Translation: BAB26282.1.
AC114645 Genomic DNA. No translation available.
BC019509 mRNA. Translation: AAH19509.1.
RefSeqNP_081410.2. NM_027134.3.
UniGeneMm.287956.

3D structure databases

ProteinModelPortalQ9D799.
SMRQ9D799. Positions 44-342.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9D799.

Proteomic databases

PRIDEQ9D799.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000074792; ENSMUSP00000074347; ENSMUSG00000059183.
GeneID69606.
KEGGmmu:69606.
UCSCuc009qdh.2. mouse.

Organism-specific databases

CTD123263.
MGIMGI:1916856. Mtfmt.

Phylogenomic databases

eggNOGCOG0223.
GeneTreeENSGT00390000017828.
HOGENOMHOG000261177.
HOVERGENHBG031552.
InParanoidQ9D799.
KOK00604.
OMATHAPKIS.
OrthoDBEOG7CZK68.
TreeFamTF323405.

Gene expression databases

BgeeQ9D799.
CleanExMM_MTFMT.
GenevestigatorQ9D799.

Family and domain databases

Gene3D3.40.50.170. 1 hit.
InterProIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR015518. Met_tRNA_Form_TA-like.
[Graphical view]
PANTHERPTHR11138. PTHR11138. 1 hit.
PfamPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMSSF53328. SSF53328. 1 hit.
TIGRFAMsTIGR00460. fmt. 1 hit.
ProtoNetSearch...

Other

NextBio329900.
PROQ9D799.
SOURCESearch...

Entry information

Entry nameFMT_MOUSE
AccessionPrimary (citable) accession number: Q9D799
Secondary accession number(s): E9QKZ0, Q8VE89
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot