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UniProtKB/Swiss-Prot entry P32785


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FMT_YEAST
Primary accession number P32785
Secondary accession number Q6RUA6
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on February 21, 2006 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 70)
Name and origin of the protein
Protein name Methionyl-tRNA formyltransferase, mitochondrial [Precursor]
Synonyms MtFMT
EC 2.1.2.9
Gene name
Name: FMT1
OrderedLocusNames: YBL013W
ORFNames: YBL0313, YBL0311
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 24657 / D273-10B, and ATCC 90840 / EAY235 / FY23;
Williams E.H., Butler C.A., Fox T.D.;
"Yeast mitochondrial translation initiation.";
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=1332308 [NCBI, ExPASy, EBI, Israel, Japan]
Skala J., van Dyck L., Purnelle B., Goffeau A.;
"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.";
Yeast 8:777-785(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[4]
FUNCTION.
DOI=10.1128/JB.182.10.2886-2892.2000; PubMed=10781559 [NCBI, ExPASy, EBI, Israel, Japan]
Li Y., Holmes W.B., Appling D.R., RajBhandary U.L.;
"Initiation of protein synthesis in Saccharomyces cerevisiae mitochondria without formylation of the initiator tRNA.";
J. Bacteriol. 182:2886-2892(2000).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1073/pnas.2135385100; PubMed=14576278 [NCBI, ExPASy, EBI, Israel, Japan]
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY490279; AAR86694.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY492339; AAR86695.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35774; CAA84832.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S25331; S25331.
RefSeq NP_009540.2; -.
3D structure databases
ModBase P32785.
Protein-protein interaction databases
DIP DIP:8221N; -.
IntAct P32785; -.
Organism-specific databases
CYGD YBL013w; -.
SGD S000000109; FMT1.
Yeast-GFP YBL013W.
Gene expression databases
ArrayExpress P32785; -.
GermOnline YBL013W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0004479; Molecular function: methionyl-tRNA formyltransferase activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006431; Biological process: methionyl-tRNA aminoacylation (inferred from direct assay from SGD).
GO:0006413; Biological process: translational initiation (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR005794; Fmt.
IPR002376; Formyl_transf_N.
IPR015518; Met_tRNA_Form_TA-like.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.170; Formyl_transf_N; 1.
PANTHER PTHR11138; Met_tRNA_Form_TA-like; 1.
Pfam PF00551; Formyl_trans_N; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00460; fmt; 1.
BLOCKS P32785.
ProtoNet P32785.
Genome annotation databases
Ensembl YBL013W; Saccharomyces cerevisiae. [Contig view]
GeneID 852270; -.
GenomeReviews Y13134_GR; YBL013W.
KEGG sce:YBL013W; -.
NMPDR fig|4932.3.peg.233; -.
Phylogenomic databases
HOGENOM P32785; -.
Other
LinkHub P32785; -.
NextBio 970878; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Methyltransferase; Mitochondrion; Protein biosynthesis; Transferase; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    26  26     Mitochondrion (Potential). 
CHAIN   27   401  375     Methionyl-tRNA formyltransferase, mitochondrial. PRO_0000010096
REGION   159   162  4     Tetrahydrofolate (THF) binding (By similarity). 
Sequence information
Length: 401 AA [This is the length of the unprocessed precursor] Molecular weight: 44617 Da [This is the MW of the unprocessed precursor] CRC64: 95E1C61C4E6D3AE1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVKMRRITPT RLLFTCRYIS NNASPPVQPL NVLFFGSDTF SNFSLQALNE LRQNNGSCGI 

        70         80         90        100        110        120 
VDNIQVVTRS PKWCGRQKSI LKYPPIFDMA EKLQLPRPIT CDTKQEMLAL SKLTPSRQGN 

       130        140        150        160        170        180 
PENDGSGAPF NAIIAVSFGK LIPGDLIRAV PLALNVHPSL LPRHKGSAPI QRALLEGDTY 

       190        200        210        220        230        240 
TGVTIQTLHP DRFDHGAIVA QTEPLAIATM LSKGRVNDST ADFNSEGLPR RTAILMDQLG 

       250        260        270        280        290        300 
ALGAQLLGQT LRERLYLPQN RVQAPTAYKP SYAHRITTED KRIHWARDSA AELLNKLETL 

       310        320        330        340        350        360 
GPLHAFKEAT AARKDAQNSV LKRILFHECK VMRDARLDNG SKPGMFKYDD IKDCILVTCR 

       370        380        390        400 
GNLLLCVSRL QFEGFAVERA GQFMARLRKR CGALSEKLVF L 

P32785 in FASTA format

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