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Q9D799

- FMT_MOUSE

UniProt

Q9D799 - FMT_MOUSE

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Protein
Methionyl-tRNA formyltransferase, mitochondrial
Gene
Mtfmt, Fmt
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 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.

Catalytic activityi

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

GO - Molecular functioni

  1. methionyl-tRNA formyltransferase activity Source: UniProtKB-EC
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
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1916856. Mtfmt.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 386Methionyl-tRNA formyltransferase, mitochondrialPRO_0000010094
Transit peptidei1 – ?Mitochondrion Reviewed prediction

Proteomic databases

PRIDEiQ9D799.

PTM databases

PhosphoSiteiQ9D799.

Expressioni

Gene expression databases

BgeeiQ9D799.
CleanExiMM_MTFMT.
GenevestigatoriQ9D799.

Structurei

3D structure databases

ProteinModelPortaliQ9D799.
SMRiQ9D799. Positions 44-342.

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.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0223.
GeneTreeiENSGT00390000017828.
HOGENOMiHOG000261177.
HOVERGENiHBG031552.
InParanoidiQ9D799.
KOiK00604.
OMAiTHAPKIS.
OrthoDBiEOG7CZK68.
TreeFamiTF323405.

Family and domain databases

Gene3Di3.40.50.170. 1 hit.
InterProiIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR015518. Met_tRNA_Form_TA-like.
[Graphical view]
PANTHERiPTHR11138. PTHR11138. 1 hit.
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

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MLLPRCCWGR WLMGRRPRCS CQAPAGFDGK DGRGSRVREK PPWRVLFLGT    50
DHFARETLRA LHAARDGKEE KLIEKLEVVT VPSLSPKGLP VKQYAIQSQL 100
PVYEWPDVGS GEYDVGVVAS FGRLLSEALI LKFPYGILNV HPSCLPRWRG 150
PAPIIHTVLH GDTVTGVTIM QIRPKRFDIG PILQQETIPV PPKSTSKELE 200
AVLSKLGANM LISVLKNLPE SLNNGRPQPA EGVTYAPKVS AGTSCVKWEE 250
QTSEQVLRLH LAIGDIVPLQ TLWMENTVKL LDLVEVNNSI LADPKLTGQT 300
VTPGFVVYHR PSQMLLVRCK DGWIGVRSVM LKKTLTATDF YNGYLHAWYQ 350
KNSHAHPSQC RFQTLRLPTK MQQKTKLLLC NSALSS 386
Length:386
Mass (Da):43,092
Last modified:July 27, 2011 - v3
Checksum:i74B0542C0ECA4D9D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401K → M in BAB26282. 1 Publication
Sequence conflicti305 – 3051F → S in AAH19509. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AK009430 mRNA. Translation: BAB26282.1 .
AC114645 Genomic DNA. No translation available.
BC019509 mRNA. Translation: AAH19509.1 .
CCDSi CCDS23292.1.
RefSeqi NP_081410.2. NM_027134.3.
UniGenei Mm.287956.

3D structure databases

ProteinModelPortali Q9D799.
SMRi Q9D799. Positions 44-342.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9D799.

Proteomic databases

PRIDEi Q9D799.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000074792 ; ENSMUSP00000074347 ; ENSMUSG00000059183 .
GeneIDi 69606.
KEGGi mmu:69606.
UCSCi uc009qdh.2. mouse.

Organism-specific databases

CTDi 123263.
MGIi MGI:1916856. Mtfmt.

Phylogenomic databases

eggNOGi COG0223.
GeneTreei ENSGT00390000017828.
HOGENOMi HOG000261177.
HOVERGENi HBG031552.
InParanoidi Q9D799.
KOi K00604.
OMAi THAPKIS.
OrthoDBi EOG7CZK68.
TreeFami TF323405.

Miscellaneous databases

NextBioi 329900.
PROi Q9D799.
SOURCEi Search...

Gene expression databases

Bgeei Q9D799.
CleanExi MM_MTFMT.
Genevestigatori Q9D799.

Family and domain databases

Gene3Di 3.40.50.170. 1 hit.
InterProi IPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR015518. Met_tRNA_Form_TA-like.
[Graphical view ]
PANTHERi PTHR11138. PTHR11138. 1 hit.
Pfami PF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view ]
SUPFAMi SSF53328. SSF53328. 1 hit.
TIGRFAMsi TIGR00460. fmt. 1 hit.
ProtoNeti Search...

Publicationsi

  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.
    , 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. 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].

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: July 9, 2014
This is version 104 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

External Data

Dasty 3

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