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Protein

Methionyl-tRNA formyltransferase, mitochondrial

Gene

FMT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Formylates methionyl-tRNA in mitochondria.1 Publication

Catalytic activityi

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

GO - Molecular functioni

  1. methionyl-tRNA formyltransferase activity Source: SGD

GO - Biological processi

  1. conversion of methionyl-tRNA to N-formyl-methionyl-tRNA Source: SGD
  2. translational initiation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciYEAST:G3O-28918-MONOMER.
BRENDAi2.1.2.9. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionyl-tRNA formyltransferase, mitochondrial (EC:2.1.2.9)
Short name:
MtFMT
Gene namesi
Name:FMT1
Ordered Locus Names:YBL013W
ORF Names:YBL0311, YBL0313
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

CYGDiYBL013w.
SGDiS000000109. FMT1.

Subcellular locationi

Mitochondrion 2 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2626MitochondrionSequence AnalysisAdd
BLAST
Chaini27 – 401375Methionyl-tRNA formyltransferase, mitochondrialPRO_0000010096Add
BLAST

Proteomic databases

PaxDbiP32785.

Expressioni

Gene expression databases

GenevestigatoriP32785.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TDH3P003591EBI-7033,EBI-7218

Protein-protein interaction databases

BioGridi32687. 55 interactions.
DIPiDIP-8221N.
IntActiP32785. 3 interactions.
MINTiMINT-4476015.
STRINGi4932.YBL013W.

Structurei

3D structure databases

ProteinModelPortaliP32785.
SMRiP32785. Positions 30-302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni159 – 1624Tetrahydrofolate (THF) bindingBy similarity

Sequence similaritiesi

Belongs to the Fmt family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0223.
GeneTreeiENSGT00390000017828.
HOGENOMiHOG000111151.
KOiK00604.
OMAiIKPTGRN.
OrthoDBiEOG7V1G2Z.

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.

P32785-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVKMRRITPT RLLFTCRYIS NNASPPVQPL NVLFFGSDTF SNFSLQALNE
60 70 80 90 100
LRQNNGSCGI VDNIQVVTRS PKWCGRQKSI LKYPPIFDMA EKLQLPRPIT
110 120 130 140 150
CDTKQEMLAL SKLTPSRQGN PENDGSGAPF NAIIAVSFGK LIPGDLIRAV
160 170 180 190 200
PLALNVHPSL LPRHKGSAPI QRALLEGDTY TGVTIQTLHP DRFDHGAIVA
210 220 230 240 250
QTEPLAIATM LSKGRVNDST ADFNSEGLPR RTAILMDQLG ALGAQLLGQT
260 270 280 290 300
LRERLYLPQN RVQAPTAYKP SYAHRITTED KRIHWARDSA AELLNKLETL
310 320 330 340 350
GPLHAFKEAT AARKDAQNSV LKRILFHECK VMRDARLDNG SKPGMFKYDD
360 370 380 390 400
IKDCILVTCR GNLLLCVSRL QFEGFAVERA GQFMARLRKR CGALSEKLVF

L
Length:401
Mass (Da):44,617
Last modified:February 21, 2006 - v2
Checksum:i95E1C61C4E6D3AE1
GO

Sequence cautioni

The sequence CAA84832.1 differs from that shown. Reason: Frameshift at position 387. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY490279 Genomic DNA. Translation: AAR86694.1.
AY492339 Genomic DNA. Translation: AAR86695.1.
Z35774 Genomic DNA. Translation: CAA84832.1. Frameshift.
BK006936 Genomic DNA. Translation: DAA07107.1.
PIRiS25331.
RefSeqiNP_009540.2. NM_001178253.1.

Genome annotation databases

EnsemblFungiiYBL013W; YBL013W; YBL013W.
GeneIDi852270.
KEGGisce:YBL013W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY490279 Genomic DNA. Translation: AAR86694.1.
AY492339 Genomic DNA. Translation: AAR86695.1.
Z35774 Genomic DNA. Translation: CAA84832.1. Frameshift.
BK006936 Genomic DNA. Translation: DAA07107.1.
PIRiS25331.
RefSeqiNP_009540.2. NM_001178253.1.

3D structure databases

ProteinModelPortaliP32785.
SMRiP32785. Positions 30-302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32687. 55 interactions.
DIPiDIP-8221N.
IntActiP32785. 3 interactions.
MINTiMINT-4476015.
STRINGi4932.YBL013W.

Proteomic databases

PaxDbiP32785.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL013W; YBL013W; YBL013W.
GeneIDi852270.
KEGGisce:YBL013W.

Organism-specific databases

CYGDiYBL013w.
SGDiS000000109. FMT1.

Phylogenomic databases

eggNOGiCOG0223.
GeneTreeiENSGT00390000017828.
HOGENOMiHOG000111151.
KOiK00604.
OMAiIKPTGRN.
OrthoDBiEOG7V1G2Z.

Enzyme and pathway databases

BioCyciYEAST:G3O-28918-MONOMER.
BRENDAi2.1.2.9. 984.

Miscellaneous databases

NextBioi970878.
PROiP32785.

Gene expression databases

GenevestigatoriP32785.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast mitochondrial translation initiation."
    Williams E.H., Butler C.A., Fox T.D.
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 24657 / D273-10B and ATCC 90840 / EAY235 / FY23.
  2. "The sequence of an 8 kb segment on the left arm of chromosome II from Saccharomyces cerevisiae identifies five new open reading frames of unknown functions, two tRNA genes and two transposable elements."
    Skala J., van Dyck L., Purnelle B., Goffeau A.
    Yeast 8:777-785(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Initiation of protein synthesis in Saccharomyces cerevisiae mitochondria without formylation of the initiator tRNA."
    Li Y., Holmes W.B., Appling D.R., RajBhandary U.L.
    J. Bacteriol. 182:2886-2892(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.

Entry informationi

Entry nameiFMT_YEAST
AccessioniPrimary (citable) accession number: P32785
Secondary accession number(s): D6VPY7, Q6RUA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 21, 2006
Last modified: January 7, 2015
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Formylation of the initiator Met-tRNA is not essential for mitochondrial protein synthesis in S.cerevisiae.
Present with 1070 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3

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 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.