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Protein

Methionyl-tRNA formyltransferase, mitochondrial

Gene

Mtfmt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Protein biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Methionyl-tRNA formyltransferase, mitochondrial (EC:2.1.2.9)
Short name:
MtFMT
Gene namesi
Name:Mtfmt
Synonyms:Fmt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1916856. Mtfmt.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000010094? – 386Methionyl-tRNA formyltransferase, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

EPDiQ9D799.
MaxQBiQ9D799.
PaxDbiQ9D799.
PRIDEiQ9D799.

PTM databases

iPTMnetiQ9D799.
PhosphoSitePlusiQ9D799.

Expressioni

Gene expression databases

BgeeiENSMUSG00000059183.
CleanExiMM_MTFMT.
GenevisibleiQ9D799. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000074347.

Structurei

3D structure databases

ProteinModelPortaliQ9D799.
SMRiQ9D799.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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 similaritiesi

Belongs to the Fmt family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3082. Eukaryota.
COG0223. LUCA.
GeneTreeiENSGT00390000017828.
HOGENOMiHOG000261177.
HOVERGENiHBG031552.
InParanoidiQ9D799.
KOiK00604.
OMAiVEGRKPM.
OrthoDBiEOG091G0QUP.
TreeFamiTF323405.

Family and domain databases

Gene3Di3.40.50.170. 1 hit.
InterProiIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
[Graphical view]
PfamiPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMiSSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D799-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLPRCCWGR WLMGRRPRCS CQAPAGFDGK DGRGSRVREK PPWRVLFLGT
60 70 80 90 100
DHFARETLRA LHAARDGKEE KLIEKLEVVT VPSLSPKGLP VKQYAIQSQL
110 120 130 140 150
PVYEWPDVGS GEYDVGVVAS FGRLLSEALI LKFPYGILNV HPSCLPRWRG
160 170 180 190 200
PAPIIHTVLH GDTVTGVTIM QIRPKRFDIG PILQQETIPV PPKSTSKELE
210 220 230 240 250
AVLSKLGANM LISVLKNLPE SLNNGRPQPA EGVTYAPKVS AGTSCVKWEE
260 270 280 290 300
QTSEQVLRLH LAIGDIVPLQ TLWMENTVKL LDLVEVNNSI LADPKLTGQT
310 320 330 340 350
VTPGFVVYHR PSQMLLVRCK DGWIGVRSVM LKKTLTATDF YNGYLHAWYQ
360 370 380
KNSHAHPSQC RFQTLRLPTK MQQKTKLLLC NSALSS
Length:386
Mass (Da):43,092
Last modified:July 27, 2011 - v3
Checksum:i74B0542C0ECA4D9D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti40K → M in BAB26282 (PubMed:16141072).Curated1
Sequence conflicti305F → S in AAH19509 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009430 mRNA. Translation: BAB26282.1.
AC114645 Genomic DNA. No translation available.
BC019509 mRNA. Translation: AAH19509.1.
CCDSiCCDS23292.1.
RefSeqiNP_081410.2. NM_027134.3.
UniGeneiMm.287956.

Genome annotation databases

EnsembliENSMUST00000074792; ENSMUSP00000074347; ENSMUSG00000059183.
GeneIDi69606.
KEGGimmu:69606.
UCSCiuc009qdh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009430 mRNA. Translation: BAB26282.1.
AC114645 Genomic DNA. No translation available.
BC019509 mRNA. Translation: AAH19509.1.
CCDSiCCDS23292.1.
RefSeqiNP_081410.2. NM_027134.3.
UniGeneiMm.287956.

3D structure databases

ProteinModelPortaliQ9D799.
SMRiQ9D799.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000074347.

PTM databases

iPTMnetiQ9D799.
PhosphoSitePlusiQ9D799.

Proteomic databases

EPDiQ9D799.
MaxQBiQ9D799.
PaxDbiQ9D799.
PRIDEiQ9D799.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000074792; ENSMUSP00000074347; ENSMUSG00000059183.
GeneIDi69606.
KEGGimmu:69606.
UCSCiuc009qdh.2. mouse.

Organism-specific databases

CTDi123263.
MGIiMGI:1916856. Mtfmt.

Phylogenomic databases

eggNOGiKOG3082. Eukaryota.
COG0223. LUCA.
GeneTreeiENSGT00390000017828.
HOGENOMiHOG000261177.
HOVERGENiHBG031552.
InParanoidiQ9D799.
KOiK00604.
OMAiVEGRKPM.
OrthoDBiEOG091G0QUP.
TreeFamiTF323405.

Miscellaneous databases

PROiQ9D799.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000059183.
CleanExiMM_MTFMT.
GenevisibleiQ9D799. MM.

Family and domain databases

Gene3Di3.40.50.170. 1 hit.
InterProiIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
[Graphical view]
PfamiPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMiSSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFMT_MOUSE
AccessioniPrimary (citable) accession number: Q9D799
Secondary accession number(s): E9QKZ0, Q8VE89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.