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P40999 (PMT1M_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
tRNA (cytosine(38)-C(5))-methyltransferase

EC=2.1.1.204
Alternative name(s):
DNA (cytosine-5)-methyltransferase-like protein 2
Short name=Dnmt2
M.SpomI
SpIM.SpoI
Gene names
Name:pmt1
ORF Names:SPBC19C2.02
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp). Can also methylate cytosine 38 in tRNA(Glu), albeit to a lower level, but not tRNA(Lys). Pmt1-dependent tRNA methylation is induced by nitrogen limitation and depends on the nutrient-sensing protein kinase sck2. Does not have DNA-methylation activity. Ref.5

Catalytic activity

S-adenosyl-L-methionine + cytosine38 in tRNA = S-adenosyl-L-homocysteine + 5-methylcytosine38 in tRNA.

Subcellular location

Cytoplasm. Nucleus Ref.4.

Induction

Constitutively expressed at protein and RNA levels. Ref.5

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.

Contains 1 SAM-dependent MTase C5-type domain.

Caution

Was originally thought not to have cytosine-5 methyltransferase activity, and this was attributed to the insertion of a Ser residue between the Pro-Cys motif found at the active site of C5 MTases (Ref.3). When this serine is deleted it becomes catalytically active and recognizes and methylates the sequence CC[AT]GG. This was in agreement with S.pombe lacking m5C DNA-methylation. However, it has later been shown that it has tRNA-methyltransferase activity despite this sequence variation (Ref.5).

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
Nucleus
   LigandRNA-binding
S-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtRNA methylation in response to nitrogen starvation

Inferred from mutant phenotype Ref.5. Source: PomBase

   Cellular_componentcytosol

Inferred from direct assay Ref.4. Source: PomBase

nucleus

Inferred from direct assay Ref.4. Source: PomBase

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA (cytosine) methyltransferase activity

Inferred from direct assay Ref.5. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330tRNA (cytosine(38)-C(5))-methyltransferase
PRO_0000088042

Regions

Domain7 – 330324SAM-dependent MTase C5-type

Sites

Active site811 By similarity

Experimental info

Mutagenesis811C → A: Loss of methyltransferase activity. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P40999 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 50A7121FA7CF58A1

FASTA33037,976
        10         20         30         40         50         60 
MLSTKRLRVL ELYSGIGGMH YALNLANIPA DIVCAIDINP QANEIYNLNH GKLAKHMDIS 

        70         80         90        100        110        120 
TLTAKDFDAF DCKLWTMSPS CQPFTRIGNR KDILDPRSQA FLNILNVLPH VNNLPEYILI 

       130        140        150        160        170        180 
ENVQGFEESK AAEECRKVLR NCGYNLIEGI LSPNQFNIPN SRSRWYGLAR LNFKGEWSID 

       190        200        210        220        230        240 
DVFQFSEVAQ KEGEVKRIRD YLEIERDWSS YMVLESVLNK WGHQFDIVKP DSSSCCCFTR 

       250        260        270        280        290        300 
GYTHLVQGAG SILQMSDHEN THEQFERNRM ALQLRYFTAR EVARLMGFPE SLEWSKSNVT 

       310        320        330 
EKCMYRLLGN SINVKVVSYL ISLLLEPLNF 

« Hide

References

« Hide 'large scale' references
[1]"The fission yeast gene pmt1+ encodes a DNA methyltransferase homologue."
Wilkinson C.R.M., Bartlett R., Nurse P., Bird A.P.
Nucleic Acids Res. 23:203-210(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: 972 / ATCC 24843.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Activation of a yeast pseudo DNA methyltransferase by deletion of a single amino acid."
Pinarbasi E., Elliott J., Hornby D.P.
J. Mol. Biol. 257:804-813(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[4]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"Pmt1, a Dnmt2 homolog in Schizosaccharomyces pombe, mediates tRNA methylation in response to nutrient signaling."
Becker M., Muller S., Nellen W., Jurkowski T.P., Jeltsch A., Ehrenhofer-Murray A.E.
Nucleic Acids Res. 40:11648-11658(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-81, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X82444 Genomic DNA. Translation: CAA57824.1.
CU329671 Genomic DNA. Translation: CAB52029.1.
PIRS53990.
RefSeqNP_595687.1. NM_001021584.2.

3D structure databases

ProteinModelPortalP40999.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid277286. 16 interactions.
MINTMINT-4689975.
STRING4896.SPBC19C2.02-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC19C2.02.1; SPBC19C2.02.1:pep; SPBC19C2.02.
GeneID2540766.
KEGGspo:SPBC19C2.02.

Organism-specific databases

PomBaseSPBC19C2.02.

Phylogenomic databases

eggNOGCOG0270.
HOGENOMHOG000265038.
KOK15336.
OMATCCFTRG.
OrthoDBEOG71K6CK.
PhylomeDBP40999.

Family and domain databases

InterProIPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
[Graphical view]
PANTHERPTHR10629. PTHR10629. 1 hit.
PfamPF00145. DNA_methylase. 1 hit.
[Graphical view]
PRINTSPR00105. C5METTRFRASE.
TIGRFAMsTIGR00675. dcm. 1 hit.
PROSITEPS00095. C5_MTASE_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20801885.
PROP40999.

Entry information

Entry namePMT1M_SCHPO
AccessionPrimary (citable) accession number: P40999
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names